Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T55781 Target Info
Target Name Tyrosine-protein kinase Mer (MERTK)
Synonyms Receptor tyrosine kinase MerTK; Proto-oncogene c-Mer
Target Type Clinical trial Target
Gene Name MERTK
Biochemical Class Kinase
UniProt ID
MERTK_HUMAN
Drug Binding Sites of Target  Top
Ligand Name: Gilteritinib Ligand Info
Structure Description Crystal structure of MerTK kinase domain in complex with Gilteritinib PDB:7AB1
Method X-ray diffraction Resolution 1.93 Å Mutation Yes [1]
PDB Sequence
SHMEELQNKL
577
EDVVIDRNLL
587
ILGRILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617

VKTMSQREIE
632
EFLSEAACMK
642
DFSHPNVIRL
652
LGVCIEMSSQ
662
GIPKPMVILP
672

FMKYGDLHTY
682
LLYSRLETGP
692
RHIPLQTLLR
702
FMVDIALGME
712
YLSNRNFLHR
722

DLAARNCMLR
732
DDMTVCVADF
742
PVKWIAIESL
772
ADRVYTSKSD
782
VWAFGVTMWE
792

IATRGMTPYP
802
GVQNHEMYDY
812
LLHGHRLKQP
822
EDCLDELYEI
832
MYSCWRTDPL
842

DRPTFSVLRL
852
QLERLLESLP
862
Residue
Distance (Å)
LEU593
3.062
GLY594
4.882
VAL601
3.682
ALA617
3.254
LYS619
4.483
ILE650
3.915
LEU671
3.738
PRO672
2.871
PHE673
3.599
MET674
2.778
Residue
Distance (Å)
LYS675
3.916
TYR676
4.856
GLY677
3.976
ASP678
3.516
TYR685
3.945
ARG727
4.159
MET730
3.280
ALA740
3.862
ASP741
3.717
Ligand Name: LY2801653 Ligand Info
Structure Description Crystal structure of MerTK kinase domain in complex with Merestinib PDB:7AAY
Method X-ray diffraction Resolution 1.87 Å Mutation No [1]
PDB Sequence
SHMEELQNKL
577
EDVVIDRNLL
587
ILGKILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617

VKTMKLDNSS
627
QREIEEFLSE
637
AACMKDFSHP
647
NVIRLLGVCI
657
EGIPKPMVIL
671

PFMKYGDLHT
681
YLLYSRLETG
691
PKHIPLQTLL
701
KFMVDIALGM
711
EYLSNRNFLH
721

RDLAARNCML
731
RDDMTVCVAD
741
FGMPVKWIAI
769
ESLADRVYTS
779
KSDVWAFGVT
789

MWEIATRGMT
799
PYPGVQNHEM
809
YDYLLHGHRL
819
KQPEDCLDEL
829
YEIMYSCWRT
839

DPLDRPTFSV
849
LRLQLEKLLE
859
SLP
Residue
Distance (Å)
LEU593
4.125
GLY594
3.820
GLU595
3.083
GLY596
4.436
VAL601
3.255
ALA617
3.396
LYS619
2.705
GLU637
3.209
ALA638
4.860
CYS640
3.922
MET641
3.335
PHE644
3.892
VAL649
3.992
ILE650
3.529
Residue
Distance (Å)
LEU671
3.388
PRO672
3.280
PHE673
3.588
MET674
2.764
GLY677
4.857
MET711
4.956
LEU714
3.039
PHE719
3.580
HIS721
3.171
MET730
3.641
VAL739
3.080
ALA740
3.638
ASP741
2.851
PHE742
3.592
Ligand Name: AZD7762 Ligand Info
Structure Description Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with AZD-7762 PDB:7CQE
Method X-ray diffraction Resolution 2.69 Å Mutation No [2]
PDB Sequence
EDVVIDRNLL
587
ILGKILGEGG
599
SVMEGNLKQE
609
DGTSLKVAVK
619
TMKREIEEFL
635

SEAACMKDFS
645
HPNVIRLLGV
655
CIEMIPKPMV
669
ILPFMKYGDL
679
HTYLLYSRLE
689

TGPKHIPLQT
699
LLKFMVDIAL
709
GMEYLSNRNF
719
LHRDLAARNC
729
MLRDDMTVCV
739

ADFGPVKWIA
768
IESLADRVYT
778
SKSDVWAFGV
788
TMWEIATRGM
798
TPYPGVQNHE
808

MYDYLLHGHR
818
LKQPEDCLDE
828
LYEIMYSCWR
838
TDPLDRPTFS
848
VLRLQLEKLL
858

ESL
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .YDJ or .YDJ2 or .YDJ3 or :3YDJ;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:596 or .A:601 or .A:617 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:730 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.673
GLY594
4.739
GLU595
3.729
GLY596
3.878
VAL601
3.744
ALA617
3.411
ILE650
4.077
LEU671
4.336
PRO672
3.244
PHE673
3.638
Residue
Distance (Å)
MET674
2.795
LYS675
3.162
TYR676
4.682
GLY677
4.010
ASP678
4.083
ARG727
2.626
ASN728
3.066
MET730
3.587
ASP741
2.786
Ligand Name: NPS-1034 Ligand Info
Structure Description MerTK kinase domain in complex with NPS-1034 PDB:7AVX
Method X-ray diffraction Resolution 2.44 Å Mutation No [3]
PDB Sequence
LEDVVIDRNL
586
LILGKILGEG
596
EFGSVMEGNL
606
KQEDGTSLKV
616
AVKTMKLDNS
626

SQREIEEFLS
636
EAACMKDFSH
646
PNVIRLLGVC
656
IEIPKPMVIL
671
PFMKYGDLHT
681

YLLYSRLETG
691
PKHIPLQTLL
701
KFMVDIALGM
711
EYLSNRNFLH
721
RDLAARNCML
731

RDDMTVCVAD
741
FGLSKKIYSG
751
DRIAKMPVKW
766
IAIESLADRV
776
YTSKSDVWAF
786

GVTMWEIATR
796
GMTPYPGVQN
806
HEMYDYLLHG
816
HRLKQPEDCL
826
DELYEIMYSC
836

WRTDPLDRPT
846
FSVLRLQLEK
856
LLESLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S4K or .S4K2 or .S4K3 or :3S4K;style chemicals stick;color identity;select .A:593 or .A:594 or .A:601 or .A:617 or .A:618 or .A:619 or .A:621 or .A:634 or .A:637 or .A:638 or .A:641 or .A:650 or .A:652 or .A:655 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:677 or .A:730 or .A:740 or .A:741 or .A:742 or .A:744; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.514
GLY594
3.948
VAL601
3.234
ALA617
3.422
VAL618
4.565
LYS619
3.414
MET621
3.367
PHE634
3.073
GLU637
3.516
ALA638
3.546
MET641
3.549
ILE650
3.544
LEU652
4.044
Residue
Distance (Å)
VAL655
4.900
VAL669
3.610
LEU671
3.330
PRO672
3.276
PHE673
3.659
MET674
2.801
LYS675
4.815
GLY677
4.270
MET730
3.398
ALA740
3.571
ASP741
3.043
PHE742
3.293
LEU744
3.618
Ligand Name: adenosine diphosphate Ligand Info
Structure Description Crystal structure of catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with ADP PDB:3BRB
Method X-ray diffraction Resolution 1.90 Å Mutation No [4]
PDB Sequence
NKLEDVVIDR
584
NLLILGKILG
594
EEFGSVMEGN
605
LKQEDGTSLK
615
VAVKTMNSSQ
628

REIEEFLSEA
638
ACMKDFSHPN
648
VIRLLGVCIE
658
KPMVILPFMK
675
YGDLHTYLLY
685

SRLETGPKHI
695
PLQTLLKFMV
705
DIALGMEYLS
715
NRNFLHRDLA
725
ARNCMLRDDM
735

TVCVADFGLS
745
MPVKWIAIES
771
LADRVYTSKS
781
DVWAFGVTMW
791
EIATRGMTPY
801

PGVQNHEMYD
811
YLLHGHRLKQ
821
PEDCLDELYE
831
IMYSCWRTDP
841
LDRPTFSVLR
851

LQLEKLLESL
861
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ADP or .ADP2 or .ADP3 or :3ADP;style chemicals stick;color identity;select .A:593 or .A:594 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:678 or .A:727 or .A:728 or .A:730 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.546
GLY594
3.719
VAL601
3.342
ALA617
3.503
LYS619
2.751
ILE650
3.817
LEU671
4.106
PRO672
2.954
Residue
Distance (Å)
PHE673
3.566
MET674
2.965
ASP678
3.574
ARG727
3.660
ASN728
3.073
MET730
3.716
ASP741
2.926
Ligand Name: AMP-PNP Ligand Info
Structure Description Catalytic Domain of the Proto-oncogene Tyrosine-protein Kinase MER PDB:2P0C
Method X-ray diffraction Resolution 2.40 Å Mutation No [4]
PDB Sequence
NKLEDVVIDR
584
NLLILGKILG
594
EFGSVMEGNL
606
KQEDGTSLKV
616
AVKTMEFLSE
637

AACMKDFSHP
647
NVIRLLGVCI
657
PKPMVILPFM
674
KYGDLHTYLL
684
YSRLETGPKH
694

IPLQTLLKFM
704
VDIALGMEYL
714
SNRNFLHRDL
724
AARNCMLRDD
734
MTVCVADFGL
744

PVKWIAIESL
772
ADRVYTSKSD
782
VWAFGVTMWE
792
IATRGMTPYP
802
GVQNHEMYDY
812

LLHGHRLKQP
822
EDCLDELYEI
832
MYSCWRTDPL
842
DRPTFSVLRL
852
QLEKLLESL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ANP or .ANP2 or .ANP3 or :3ANP;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:677 or .A:678 or .A:723 or .A:727 or .A:728 or .A:730 or .A:741; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.597
GLY594
3.623
GLU595
4.701
VAL601
3.255
ALA617
3.505
LYS619
4.770
ILE650
3.814
LEU671
4.231
PRO672
2.763
Residue
Distance (Å)
PHE673
3.612
MET674
2.888
GLY677
4.989
ASP678
3.704
ASP723
3.291
ARG727
3.242
ASN728
2.748
MET730
3.556
ASP741
2.661
Ligand Name: UNC569 Ligand Info
Structure Description Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC569 PDB:3TCP
Method X-ray diffraction Resolution 2.69 Å Mutation No [5]
PDB Sequence
LEDVVIDRNL
586
LILGKILGSV
601
MEGNLKQEDG
611
TSLKVAVKTM
621
KLDNSSQREI
631

EEFLSEAACM
641
KDFSHPNVIR
651
LLGVCIEPKP
667
MVILPFMKYG
677
DLHTYLLYSR
687

LETGPKHIPL
697
QTLLKFMVDI
707
ALGMEYLSNR
717
NFLHRDLAAR
727
NCMLRDDMTV
737

CVADFPVKWI
767
AIESLADRVY
777
TSKSDVWAFG
787
VTMWEIATRG
797
MTPYPGVQNH
807

EMYDYLLHGH
817
RLKQPEDCLD
827
ELYEIMYSCW
837
RTDPLDRPTF
847
SVLRLQLEKL
857

LESLPD
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CKJ or .CKJ2 or .CKJ3 or :3CKJ;style chemicals stick;color identity;select .A:593 or .A:594 or .A:601 or .A:617 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.809
GLY594
4.350
VAL601
3.601
ALA617
3.543
ILE650
3.982
LEU671
3.803
PRO672
3.070
PHE673
3.732
MET674
2.876
Residue
Distance (Å)
LYS675
3.173
TYR676
4.655
GLY677
3.664
ASP678
3.927
ARG727
2.675
ASN728
3.312
MET730
3.471
ALA740
3.982
ASP741
4.475
Ligand Name: LDC1267 Ligand Info
Structure Description Crystal structure of MerTK kinase domain in complex with LDC1267 PDB:7AAX
Method X-ray diffraction Resolution 1.76 Å Mutation Yes [1]
PDB Sequence
GSHMEELQNK
576
LEDVVIDRNL
586
LILGRILGEG
596
EFGSVMEGNL
606
KQEDGTSLKV
616

AVKTMSQREI
631
EEFLSEAACM
641
KDFSHPNVIR
651
LLGVCIEMSS
661
QGIPKPMVIL
671

PFMKYGDLHT
681
YLLYSRLETG
691
PRHIPLQTLL
701
RFMVDIALGM
711
EYLSNRNFLH
721

RDLAARNCML
731
RDDMTVCVAD
741
FPVKWIAIES
771
LADRVYTSKS
781
DVWAFGVTMW
791

EIATRGMTPY
801
PGVQNHEMYD
811
YLLHGHRLKQ
821
PEDCLDELYE
831
IMYSCWRTDP
841

LDRPTFSVLR
851
LQLERLLESL
861
P
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set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .R6H or .R6H2 or .R6H3 or :3R6H;style chemicals stick;color identity;select .A:593 or .A:594 or .A:601 or .A:617 or .A:618 or .A:619 or .A:634 or .A:637 or .A:638 or .A:641 or .A:650 or .A:652 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:714 or .A:719 or .A:721 or .A:730 or .A:739 or .A:740 or .A:741 or .A:742; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.789
GLY594
4.540
VAL601
3.437
ALA617
3.428
VAL618
4.395
LYS619
3.363
PHE634
3.134
GLU637
4.009
ALA638
4.200
MET641
3.652
ILE650
3.489
LEU652
3.049
VAL669
3.759
LEU671
3.351
Residue
Distance (Å)
PRO672
3.220
PHE673
3.806
MET674
2.906
LYS675
3.520
TYR676
4.935
GLY677
4.114
LEU714
4.945
PHE719
4.630
HIS721
3.958
MET730
3.528
VAL739
4.210
ALA740
3.246
ASP741
3.009
PHE742
3.409
Ligand Name: UNC2025 Ligand Info
Structure Description Crystal structure of MerTK kinase domain in complex with UNC2025 PDB:7AB2
Method X-ray diffraction Resolution 1.78 Å Mutation Yes [1]
PDB Sequence
SHMEELQNKL
577
EDVVIDRNLL
587
ILGRILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617

VKTMSQREIE
632
EFLSEAACMK
642
DFSHPNVIRL
652
LGVCIEMSSQ
662
GIPKPMVILP
672

FMKYGDLHTY
682
LLYSRLETGP
692
RHIPLQTLLR
702
FMVDIALGME
712
YLSNRNFLHR
722

DLAARNCMLR
732
DDMTVCVADF
742
PVKWIAIESL
772
ADRVYTSKSD
782
VWAFGVTMWE
792

IATRGMTPYP
802
GVQNHEMYDY
812
LLHGHRLKQP
822
EDCLDELYEI
832
MYSCWRTDPL
842

DRPTFSVLRL
852
QLERLLESLP
862
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .R6N or .R6N2 or .R6N3 or :3R6N;style chemicals stick;color identity;select .A:593 or .A:601 or .A:617 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
4.305
VAL601
3.805
ALA617
3.651
ILE650
4.215
LEU671
3.525
PRO672
2.966
PHE673
3.241
MET674
2.794
Residue
Distance (Å)
LYS675
3.278
TYR676
4.550
GLY677
4.674
ASP678
3.907
ARG727
4.492
MET730
3.751
ALA740
4.382
ASP741
4.585
Ligand Name: (10r)-7-Amino-11-Chloro-12-Fluoro-1-(2-Hydroxyethyl)-3,10,16-Trimethyl-16,17-Dihydro-1h-8,4-(Azeno)pyrazolo[4,3-H][2,5,11]benzoxadiazacyclotetradecin-15(10h)-One Ligand Info
Structure Description Crystal structure of the Mer kinase domain in complex with a macrocyclic inhibitor PDB:5U6C
Method X-ray diffraction Resolution 2.10 Å Mutation No [6]
PDB Sequence
ELQNKLEDVV
581
IDRNLLILGK
591
ILGEGEFGSV
601
MEGNLKQEDG
611
TSLKVAVKTM
621

KLDNSSQREI
631
EEFLSEAACM
641
KDFSHPNVMR
651
LLGVCIEMIP
665
KPMVILPFMK
675

YGDLHTYLLY
685
SRLETGPKHI
695
PLQTLLKFMV
705
DIALGMEYLS
715
NRNFLHRDLA
725

ARNCMLRDDM
735
TVCVADFGLS
745
PVKWIAIESL
772
ADRVYTSKSD
782
VWAFGVTMWE
792

IATRGMTPYP
802
GVQNHEMYDY
812
LLHGHRLKQP
822
EDCLDELYEI
832
MYSCWRTDPL
842

DRPTFSVLRL
852
QLEKLLESLP
862
DV
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .7YS or .7YS2 or .7YS3 or :37YS;style chemicals stick;color identity;select .A:593 or .A:594 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:677 or .A:678 or .A:681 or .A:727 or .A:728 or .A:729 or .A:730 or .A:740 or .A:741; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.576
GLY594
4.099
VAL601
3.397
ALA617
3.387
LYS619
4.333
MET650
3.454
LEU671
3.696
PRO672
2.834
PHE673
3.506
MET674
2.968
Residue
Distance (Å)
LYS675
4.503
GLY677
3.328
ASP678
2.666
THR681
4.469
ARG727
3.181
ASN728
3.365
CYS729
4.497
MET730
3.489
ALA740
3.355
ASP741
3.931
Ligand Name: N-(2-{4-[(2s)-4-(Methylsulfonyl)morpholin-2-Yl]-1,3-Thiazol-2-Yl}phenyl)-1h-Imidazole-2-Carboxamide Ligand Info
Structure Description Structure-based optimization of 1H-imidazole-2-carboxamides as Axl kinase inhibitors utilizing a Mer mutant surrogate PDB:5TC0
Method X-ray diffraction Resolution 2.24 Å Mutation No [7]
PDB Sequence
EDVVIDRNLL
587
ILGKILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617
VKTMKDFSHP
647

NVMRLLGVCI
657
EMSSQGIPKP
667
MVILPFMKYG
677
DLHTYLLYSR
687
LETGPKHIPL
697

QTLLKFMVDI
707
ALGMEYLSNR
717
NFLHRDLAAR
727
NCMLRDDMTV
737
CVADFMPVKW
766

IAIETSKSDV
783
WAFGVTMWEI
793
ATRGMTPYPG
803
VQNHEMYDYL
813
LHGHRLKQPE
823

DCLDELYEIM
833
YSCWRTDPLD
843
RPTFSVLRLQ
853
LEKLLESL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .79Y or .79Y2 or .79Y3 or :379Y;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:596 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:729 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
4.031
GLY594
4.069
GLU595
3.738
GLY596
3.887
VAL601
3.600
ALA617
3.264
LYS619
2.913
MET650
3.386
LEU671
3.477
PRO672
2.964
PHE673
3.625
Residue
Distance (Å)
MET674
2.702
LYS675
3.925
TYR676
4.944
GLY677
3.654
ASP678
3.731
ARG727
3.870
ASN728
3.640
CYS729
4.974
MET730
3.654
ALA740
3.707
ASP741
3.327
Ligand Name: Unk-D-hPhe-bAla(3S-Ph(4-CF3))-NHMe Ligand Info
Structure Description MerTK kinase domain with type 3 inhibitor from a DNA-encoded library PDB:7AW4
Method X-ray diffraction Resolution 1.98 Å Mutation No [3]
PDB Sequence
KLEDVVIDRN
585
LLILGKILGE
595
GEFGSVMEGN
605
LKQEDGTSLK
615
VAVKTMKLDN
625

SSQREIEEFL
635
SEAACMKDFS
645
HPNVIRLLGV
655
CIEPKPMVIL
671
PFMKYGDLHT
681

YLLYSRLETG
691
PKHIPLQTLL
701
KFMVDIALGM
711
EYLSNRNFLH
721
RDLAARNCML
731

RDDMTVCVAD
741
FGLSPVKWIA
768
IESLADRVYT
778
SKSDVWAFGV
788
TMWEIATRGM
798

TPYPGVQNHE
808
MYDYLLHGHR
818
LKQPEDCLDE
828
LYEIMYSCWR
838
TDPLDRPTFS
848

VLRLQLEKLL
858
ESLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S5E or .S5E2 or .S5E3 or :3S5E;style chemicals stick;color identity;select .A:619 or .A:621 or .A:623 or .A:630 or .A:633 or .A:634 or .A:637 or .A:638 or .A:641 or .A:649 or .A:650 or .A:652 or .A:669 or .A:671 or .A:714 or .A:719 or .A:720 or .A:721 or .A:722 or .A:739 or .A:740 or .A:741 or .A:742; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS619
2.922
MET621
3.271
LEU623
3.702
GLU630
3.662
GLU633
3.493
PHE634
3.590
GLU637
2.794
ALA638
3.961
MET641
3.344
VAL649
3.945
ILE650
3.128
LEU652
3.730
Residue
Distance (Å)
VAL669
3.650
LEU671
3.617
LEU714
3.416
PHE719
3.939
LEU720
3.804
HIS721
3.172
ARG722
3.677
VAL739
3.504
ALA740
3.460
ASP741
2.977
PHE742
4.897
Ligand Name: (7s)-7-Amino-N-[(4-Fluorophenyl)methyl]-8-Oxo-2,9,16,18,21-Pentaazabicyclo[15.3.1]henicosa-1(21),17,19-Triene-20-Carboxamide Ligand Info
Structure Description Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC2541 PDB:5K0X
Method X-ray diffraction Resolution 2.23 Å Mutation No [8]
PDB Sequence
KLEDVVIDRN
585
LLILGKILGE
595
GSVMEGNLKQ
608
EDGTSLKVAV
618
KTMKLDNSSQ
628

IEEFLSEAAC
640
MKDFSHPNVI
650
RLLGVCIEPK
666
PMVILPFMKY
676
GDLHTYLLYS
686

RLETGPKHIP
696
LQTLLKFMVD
706
IALGMEYLSN
716
RNFLHRDLAA
726
RNCMLRDDMT
736

VCVADFGPVK
765
WIAIESLADR
775
VYTSKSDVWA
785
FGVTMWEIAT
795
RGMTPYPGVQ
805

NHEMYDYLLH
815
GHRLKQPEDC
825
LDELYEIMYS
835
CWRTDPLDRP
845
TFSVLRLQLE
855

KLLESLPD
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .K0X or .K0X2 or .K0X3 or :3K0X;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:599 or .A:601 or .A:603 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
2.068
GLY594
3.212
GLU595
3.369
GLY599
4.765
VAL601
2.105
GLU603
4.728
ALA617
2.667
LYS619
2.263
ILE650
2.669
LEU671
2.369
PRO672
2.364
Residue
Distance (Å)
PHE673
2.763
MET674
2.294
LYS675
2.517
TYR676
4.305
GLY677
3.116
ASP678
2.634
ARG727
2.570
ASN728
2.914
MET730
2.576
ALA740
2.518
ASP741
2.261
Ligand Name: N-Butyl-2-(Butylamino)-4-[(Trans-4-Hydroxycyclohexyl)amino]-N-Methylpyrimidine-5-Carboxamide Ligand Info
Structure Description Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC1896 PDB:4MH7
Method X-ray diffraction Resolution 2.51 Å Mutation No [9]
PDB Sequence
LEDVVIDRNL
586
LILGKILGEG
596
EFGSVMEGNL
606
KQEDGTSLKV
616
AVKTAACMKD
643

FSHPNVIRLL
653
GVCIEMSSQG
663
IPKPMVILPF
673
MKYGDLHTYL
683
LYSRLETGPK
693

HIPLQTLLKF
703
MVDIALGMEY
713
LSNRNFLHRD
723
LAARNCMLRD
733
DMTVCVADFP
763

VKWIAIESLA
773
DRVYTSKSDV
783
WAFGVTMWEI
793
ATRGMTPYPG
803
VQNHEMYDYL
813

LHGHRLKQPE
823
DCLDELYEIM
833
YSCWRTDPLD
843
RPTFSVLRLQ
853
LEKLLESL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MH7 or .MH72 or .MH73 or :3MH7;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:596 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:681 or .A:685 or .A:727 or .A:728 or .A:730 or .A:740 or .A:741; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.159
GLY594
2.397
GLU595
3.097
GLY596
3.504
VAL601
2.223
ALA617
1.986
LYS619
2.899
ILE650
2.383
LEU671
2.833
PRO672
2.901
PHE673
2.539
MET674
2.288
Residue
Distance (Å)
LYS675
2.320
TYR676
2.979
GLY677
2.640
ASP678
3.885
THR681
4.921
TYR685
3.339
ARG727
4.413
ASN728
4.009
MET730
2.383
ALA740
2.680
ASP741
2.826
Ligand Name: traazacyclotetradecin-8(3H)-one Ligand Info
Structure Description Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC2434 PDB:5K0K
Method X-ray diffraction Resolution 2.54 Å Mutation No [10]
PDB Sequence
LEDVVIDRNL
586
LILGKILGEG
599
SVMEGNLKQE
609
DGTSLKVAVK
619
TMKLDNSSQR
629

EIEEFLSEAA
639
CMKDFSHPNV
649
IRLLGVCIEP
665
KPMVILPFMK
675
YGDLHTYLLY
685

SRLETGPKHI
695
PLQTLLKFMV
705
DIALGMEYLS
715
NRNFLHRDLA
725
ARNCMLRDDM
735

TVCVADFGLP
763
VKWIAIESLA
773
DRVYTSKSDV
783
WAFGVTMWEI
793
ATRGMTPYPG
803

VQNHEMYDYL
813
LHGHRLKQPE
823
DCLDELYEIM
833
YSCWRTDPLD
843
RPTFSVLRLQ
853

LEKLLESLPD
863
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .6Q1 or .6Q12 or .6Q13 or :36Q1;style chemicals stick;color identity;select .A:591 or .A:593 or .A:594 or .A:601 or .A:603 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:729 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS591
3.087
LEU593
2.845
GLY594
4.168
VAL601
2.893
GLU603
4.594
ALA617
2.599
LYS619
3.838
ILE650
2.585
LEU671
2.270
PRO672
2.237
PHE673
2.907
Residue
Distance (Å)
MET674
2.277
LYS675
2.666
TYR676
4.525
GLY677
2.958
ASP678
2.551
ARG727
2.612
ASN728
2.567
CYS729
4.761
MET730
2.343
ALA740
2.329
ASP741
2.736
Ligand Name: 2-(Butylamino)-4-[(Trans-4-Hydroxycyclohexyl)amino]-N-(4-Sulfamoylbenzyl)pyrimidine-5-Carboxamide Ligand Info
Structure Description Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC1817 PDB:4MHA
Method X-ray diffraction Resolution 2.59 Å Mutation No [9]
PDB Sequence
VVIDRNLLIL
589
GKILGEGSVM
602
EGNLKQEDGT
612
SLKVAVKTMK
622
LDNSSQREIE
632

EFLSEAACMK
642
DFSHPNVIRL
652
LGVCIEPKPM
668
VILPFMKYGD
678
LHTYLLYSRL
688

ETGPKHIPLQ
698
TLLKFMVDIA
708
LGMEYLSNRN
718
FLHRDLAARN
728
CMLRDDMTVC
738

VADFGPVKWI
767
AIESLADRVY
777
TSKSDVWAFG
787
VTMWEIATRG
797
MTPYPGVQNH
807

EMYDYLLHGH
817
RLKQPEDCLD
827
ELYEIMYSCW
837
RTDPLDRPTF
847
SVLRLQLEKL
857

LESLPD
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4MH or .4MH2 or .4MH3 or :34MH;style chemicals stick;color identity;select .A:591 or .A:593 or .A:594 or .A:595 or .A:601 or .A:603 or .A:615 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:730 or .A:740 or .A:741; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS591
3.667
LEU593
2.078
GLY594
2.465
GLU595
4.316
VAL601
2.698
GLU603
3.615
LYS615
3.490
ALA617
2.047
LYS619
3.924
ILE650
2.453
LEU671
2.622
PRO672
2.743
Residue
Distance (Å)
PHE673
2.587
MET674
2.150
LYS675
2.490
TYR676
4.027
GLY677
2.875
ASP678
3.416
ARG727
3.560
ASN728
4.058
MET730
2.287
ALA740
2.357
ASP741
2.521
Ligand Name: Trans-4-{[2-(Butylamino)-5-(Pyridin-2-Yl)pyrimidin-4-Yl]amino}cyclohexanol Ligand Info
Structure Description Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC1917 PDB:4M3Q
Method X-ray diffraction Resolution 2.72 Å Mutation No [11]
PDB Sequence
EDVVIDRNLL
587
ILGKILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617
VKTCMKDFSH
646

PNVIRLLGVC
656
IEMSSQGIPK
666
PMVILPFMKY
676
GDLHTYLLYS
686
RLETGPKHIP
696

LQTLLKFMVD
706
IALGMEYLSN
716
RNFLHRDLAA
726
RNCMLRDDMT
736
VCVADFPVKW
766

IAIESLRVYT
778
SKSDVWAFGV
788
TMWEIATRGM
798
TPYPGVQNHE
808
MYDYLLHGHR
818

LKQPEDCLDE
828
LYEIMYSCWR
838
TDPLDRPTFS
848
VLRLQLEKLL
858
ESL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .24K or .24K2 or .24K3 or :324K;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:596 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
2.525
GLY594
2.332
GLU595
3.158
GLY596
3.653
VAL601
2.240
ALA617
2.254
LYS619
3.939
ILE650
2.904
LEU671
2.542
PRO672
2.371
PHE673
2.966
Residue
Distance (Å)
MET674
2.309
LYS675
2.851
TYR676
4.194
GLY677
2.760
ASP678
2.866
ARG727
3.842
ASN728
4.376
MET730
2.352
ALA740
2.346
ASP741
2.938
Ligand Name: 2-(2-Hydroxyethylamino)-6-(3-chloroanilino)-9-isopropylpurine Ligand Info
Structure Description Crystal structure of catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor C52 PDB:3BPR
Method X-ray diffraction Resolution 2.80 Å Mutation No [4]
PDB Sequence
NKLEDVVIDR
584
NLLILGKILG
594
EGEFGSVMEG
604
NLKQEDGTSL
614
KVAVKTMKRE
630

IEEFLSEAAC
640
MKDFSHPNVI
650
RLLGVCIEMS
660
SPMVILPFMK
675
YGDLHTYLLY
685

SRLETGPKHI
695
PLQTLLKFMV
705
DIALGMEYLS
715
NRNFLHRDLA
725
ARNCMLRDDM
735

TVCVADFGLS
745
PVKWIAIESL
772
ADRVYTSKSD
782
VWAFGVTMWE
792
IATRGMTPYP
802

GVQNHEMYDY
812
LLHGHRLKQP
822
EDCLDELYEI
832
MYSCWRTDPL
842
DRPTFSVLRL
852

QLEKLLESLP
862
D
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OLP or .OLP2 or .OLP3 or :3OLP;style chemicals stick;color identity;select .A:593 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:681 or .A:730 or .A:740 or .A:741; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.750
VAL601
3.829
ALA617
3.482
LYS619
4.088
ILE650
4.301
LEU671
4.147
PRO672
3.382
PHE673
3.507
MET674
2.622
Residue
Distance (Å)
LYS675
2.702
TYR676
4.193
GLY677
3.441
ASP678
2.712
THR681
4.862
MET730
3.249
ALA740
4.013
ASP741
4.647
Ligand Name: 2-(butylamino)-N-[1-(3-fluoropropyl)piperidin-4-yl]-4-{[(1r,4r)-4-hydroxycyclohexyl]amino}pyrimidine-5-carboxamide Ligand Info
Structure Description Crystal Structure of the MerTK Kinase Domain in Complex with Inhibitor MIPS15692 PDB:7M5Z
Method X-ray diffraction Resolution 3.06 Å Mutation No [12]
PDB Sequence
LEDVVIDRNL
586
LILGRILGEG
596
EFGSVMEGNL
606
KQEDGTSLKV
616
AVKTMNSSQR
629

EIEEFLSEAA
639
CMKDFSHPNV
649
IRLLGVCIEM
659
SSQGIPKPMV
669
ILPFMKYGDL
679

HTYLLYSRLE
689
TGPRHIPLQT
699
LLRFMVDIAL
709
GMEYLSNRNF
719
LHRDLAARNC
729

MLRDDMTVCV
739
ADFPVKWIAI
769
ESLADRVYTS
779
KSDVWAFGVT
789
MWEIATRGMT
799

PYPGVQNHEM
809
YDYLLHGHRL
819
KQPEDCLDEL
829
YEIMYSCWRT
839
DPLDRPTFSV
849

LRLQLERLLE
859
SLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .YR7 or .YR72 or .YR73 or :3YR7;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:596 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.949
GLY594
3.822
GLU595
4.213
GLY596
4.681
VAL601
3.551
ALA617
3.277
LYS619
3.672
ILE650
3.968
LEU671
3.869
PRO672
3.354
Residue
Distance (Å)
PHE673
3.845
MET674
2.812
LYS675
3.146
TYR676
4.186
GLY677
3.603
ASP678
3.909
ARG727
4.610
MET730
3.562
ALA740
4.079
ASP741
4.672
Ligand Name: 2-(cyclopentyloxy)-9-(2,6-difluorobenzyl)-N-methyl-9H-purin-6-amine Ligand Info
Structure Description MerTK kinase domain in complex with purine inhibitor PDB:7AW0
Method X-ray diffraction Resolution 1.89 Å Mutation Yes [3]
PDB Sequence
SHMEELQNKL
577
EDVVIDRNLL
587
ILGRILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617

VKTMQREIEE
633
FLSEAACMKD
643
FSHPNVIRLL
653
GVCIEMSSQG
663
IPKPMVILPF
673

MKYGDLHTYL
683
LYSRLETGPR
693
HIPLQTLLRF
703
MVDIALGMEY
713
LSNRNFLHRD
723

LAARNCMLRD
733
DMTVCVADFP
763
VKWIAIESLA
773
DRVYTSKSDV
783
WAFGVTMWEI
793

ATRGMTPYPG
803
VQNHEMYDYL
813
LHGHRLKQPE
823
DCLDELYEIM
833
YSCWRTDPLD
843

RPTFSVLRLQ
853
LERLLESLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S4Q or .S4Q2 or .S4Q3 or :3S4Q;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:596 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:730 or .A:740 or .A:741; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.689
GLY594
3.563
GLU595
4.226
GLY596
4.694
VAL601
3.396
ALA617
3.417
LYS619
4.380
ILE650
3.120
LEU671
3.661
Residue
Distance (Å)
PRO672
3.123
PHE673
3.669
MET674
2.700
LYS675
3.979
TYR676
4.982
GLY677
3.814
MET730
3.284
ALA740
3.791
ASP741
3.382
Ligand Name: 5-[4-(1,5-dimethylpyrazol-4-yl)-2-methylphenyl]-N-(imidazo[1,2-a]pyridin-6-ylmethyl)-N-methyl-1,3,4-oxadiazol-2-amine Ligand Info
Structure Description MerTK kinase domain with type 1.5 inhibitor containing a di-methyl pyrazole group PDB:7OLS
Method X-ray diffraction Resolution 1.89 Å Mutation Yes [13]
PDB Sequence
GSHMEELQNK
576
LEDVVIDRNL
586
LILGRILGEG
596
EFGSVMEGNL
606
KQEDGTSLKV
616

AVKTMSSQRE
630
IEEFLSEAAC
640
MKDFSHPNVI
650
RLLGVCIEMS
660
SQGIPKPMVI
670

LPFMKYGDLH
680
TYLLYSRLET
690
GPRHIPLQTL
700
LRFMVDIALG
710
MEYLSNRNFL
720

HRDLAARNCM
730
LRDDMTVCVA
740
DFGPVKWIAI
769
ESLADRVYTS
779
KSDVWAFGVT
789

MWEIATRGMT
799
PYPGVQNHEM
809
YDYLLHGHRL
819
KQPEDCLDEL
829
YEIMYSCWRT
839

DPLDRPTFSV
849
LRLQLERLLE
859
SLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .VJZ or .VJZ2 or .VJZ3 or :3VJZ;style chemicals stick;color identity;select .A:593 or .A:601 or .A:617 or .A:619 or .A:621 or .A:634 or .A:637 or .A:638 or .A:641 or .A:650 or .A:652 or .A:655 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:730 or .A:740 or .A:741 or .A:742; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
4.459
VAL601
3.811
ALA617
3.547
LYS619
4.098
MET621
4.530
PHE634
3.153
GLU637
3.690
ALA638
3.505
MET641
3.651
ILE650
3.747
LEU652
3.894
Residue
Distance (Å)
VAL655
4.778
VAL669
3.992
LEU671
3.232
PRO672
3.566
PHE673
3.644
MET674
2.916
MET730
3.573
ALA740
3.603
ASP741
2.941
PHE742
3.621
Ligand Name: N-[6-[4-[[4-(6,8-dihydro-5H-imidazo[1,2-a]pyrazin-7-ylmethyl)-3-(trifluoromethyl)phenyl]carbamoylamino]phenoxy]pyrimidin-4-yl]cyclopropanecarboxamide Ligand Info
Structure Description MerTK kinase domain in complex with a type 2 inhibitor PDB:7AW1
Method X-ray diffraction Resolution 1.98 Å Mutation Yes [3]
PDB Sequence
SHMEELQNKL
577
EDVVIDRNLL
587
ILGRILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617

VKTMSQREIE
632
EFLSEAACMK
642
DFSHPNVIRL
652
LGVCIEMSSI
664
PKPMVILPFM
674

KYGDLHTYLL
684
YSRLETGPRH
694
IPLQTLLRFM
704
VDIALGMEYL
714
SNRNFLHRDL
724

AARNCMLRDD
734
MTVCVADFPV
764
KWIAIESLAD
774
RVYTSKSDVW
784
AFGVTMWEIA
794

TRGMTPYPGV
804
QNHEMYDYLL
814
HGHRLKQPED
824
CLDELYEIMY
834
SCWRTDPLDR
844

PTFSVLRLQL
854
ERLLESLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S4T or .S4T2 or .S4T3 or :3S4T;style chemicals stick;color identity;select .A:593 or .A:601 or .A:617 or .A:619 or .A:637 or .A:641 or .A:644 or .A:649 or .A:650 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:714 or .A:719 or .A:720 or .A:721 or .A:722 or .A:730 or .A:739 or .A:740 or .A:741 or .A:742; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
4.220
VAL601
3.814
ALA617
3.405
LYS619
3.760
GLU637
3.234
MET641
3.578
PHE644
3.557
VAL649
4.388
ILE650
3.599
VAL669
4.579
LEU671
3.287
PRO672
3.282
PHE673
3.743
MET674
2.949
Residue
Distance (Å)
LYS675
3.788
TYR676
4.560
GLY677
3.761
LEU714
4.567
PHE719
3.402
LEU720
4.676
HIS721
3.586
ARG722
4.518
MET730
3.548
VAL739
3.672
ALA740
3.445
ASP741
2.880
PHE742
3.383
Ligand Name: N-[[3-[4-[(dimethylamino)methyl]phenyl]imidazo[1,2-a]pyridin-6-yl]methyl]-N-methyl-5-[3-methyl-5-(1,3,5-trimethylpyrazol-4-yl)pyridin-2-yl]-1,3,4-oxadiazol-2-amine Ligand Info
Structure Description MerTK kinase domain with type 1.5 inhibitor containing a tri-methyl pyrazole group PDB:7OLX
Method X-ray diffraction Resolution 1.98 Å Mutation Yes [13]
PDB Sequence
GSHMEELQNK
576
LEDVVIDRNL
586
LILGRILGEG
596
EFGSVMEGNL
606
KQEDGTSLKV
616

AVKTMKNSSQ
628
REIEEFLSEA
638
ACMKDFSHPN
648
VIRLLGVCIE
658
MSSQGIPKPM
668

VILPFMKYGD
678
LHTYLLYSRL
688
ETGPRHIPLQ
698
TLLRFMVDIA
708
LGMEYLSNRN
718

FLHRDLAARN
728
CMLRDDMTVC
738
VADFGPVKWI
767
AIESLADRVY
777
TSKSDVWAFG
787

VTMWEIATRG
797
MTPYPGVQNH
807
EMYDYLLHGH
817
RLKQPEDCLD
827
ELYEIMYSCW
837

RTDPLDRPTF
847
SVLRLQLERL
857
LESLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .VK5 or .VK52 or .VK53 or :3VK5;style chemicals stick;color identity;select .A:593 or .A:594 or .A:601 or .A:617 or .A:619 or .A:621 or .A:634 or .A:637 or .A:638 or .A:641 or .A:650 or .A:652 or .A:655 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:677 or .A:678 or .A:681 or .A:730 or .A:740 or .A:741 or .A:742 or .A:743; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.672
GLY594
4.338
VAL601
3.762
ALA617
3.604
LYS619
3.201
MET621
3.782
PHE634
3.113
GLU637
3.725
ALA638
3.575
MET641
3.447
ILE650
3.649
LEU652
3.871
VAL655
4.550
Residue
Distance (Å)
VAL669
3.827
LEU671
3.306
PRO672
3.428
PHE673
3.650
MET674
2.885
GLY677
4.319
ASP678
4.639
THR681
4.800
MET730
3.437
ALA740
3.553
ASP741
2.900
PHE742
3.580
GLY743
4.358
Ligand Name: 2-[1-[[(5-chloro-1H-pyrrolo[2,3-b]pyridine-3-carbonyl)amino]methyl]-2-azabicyclo[2.1.1]hexan-2-yl]-N-methyl-4-(trifluoromethyl)-1,3-thiazole-5-carboxamide Ligand Info
Structure Description MerTK kinase domain with type 1 inhibitor from a DNA-encoded library PDB:7AW3
Method X-ray diffraction Resolution 1.99 Å Mutation Yes [3]
PDB Sequence
SHMEELQNKL
577
EDVVIDRNLL
587
ILGRILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617

VKTMQREIEE
633
FLSEAACMKD
643
FSHPNVIRLL
653
GVCIEMSSQG
663
IPKPMVILPF
673

MKYGDLHTYL
683
LYSRLETGPR
693
HIPLQTLLRF
703
MVDIALGMEY
713
LSNRNFLHRD
723

LAARNCMLRD
733
DMTVCVADFP
763
VKWIAIESLA
773
DRVYTSKSDV
783
WAFGVTMWEI
793

ATRGMTPYPG
803
VQNHEMYDYL
813
LHGHRLKQPE
823
DCLDELYEIM
833
YSCWRTDPLD
843

RPTFSVLRLQ
853
LERLLESLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S4Z or .S4Z2 or .S4Z3 or :3S4Z;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:677 or .A:678 or .A:681 or .A:727 or .A:728 or .A:730 or .A:740 or .A:741; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.484
GLY594
3.169
GLU595
4.807
VAL601
3.214
ALA617
3.394
LYS619
4.745
ILE650
3.847
LEU671
3.238
PRO672
2.712
PHE673
3.669
Residue
Distance (Å)
MET674
2.821
GLY677
4.737
ASP678
2.907
THR681
3.574
ARG727
3.039
ASN728
3.439
MET730
3.200
ALA740
4.244
ASP741
3.518
Ligand Name: 2-N-[4-(cyclopropylmethoxy)-3,5-difluorophenyl]-5-[(3R)-3-methylpiperazin-1-yl]-4-N-(oxan-4-yl)pyrimidine-2,4-diamine Ligand Info
Structure Description MerTK kinase domain in complex with a bisaminopyrimidine inhibitor PDB:7AVZ
Method X-ray diffraction Resolution 2.04 Å Mutation Yes [3]
PDB Sequence
SHMEELQNKL
577
EDVVIDRNLL
587
ILGRILGEGE
597
FGSVMEGNLK
607
QEDGTSLKVA
617

VKTMSQREIE
632
EFLSEAACMK
642
DFSHPNVIRL
652
LGVCIEMSSI
664
PKPMVILPFM
674

KYGDLHTYLL
684
YSRLETGPRH
694
IPLQTLLRFM
704
VDIALGMEYL
714
SNRNFLHRDL
724

AARNCMLRDD
734
MTVCVADFPV
764
KWIAIESLAD
774
RVYTSKSDVW
784
AFGVTMWEIA
794

TRGMTPYPGV
804
QNHEMYDYLL
814
HGHRLKQPED
824
CLDELYEIMY
834
SCWRTDPLDR
844

PTFSVLRLQL
854
ERLLESLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S4N or .S4N2 or .S4N3 or :3S4N;style chemicals stick;color identity;select .A:593 or .A:594 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:729 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.774
GLY594
4.694
VAL601
3.495
ALA617
3.246
LYS619
4.104
ILE650
3.320
LEU671
3.404
PRO672
3.068
PHE673
3.627
MET674
2.815
Residue
Distance (Å)
LYS675
3.723
TYR676
4.718
GLY677
3.794
ASP678
3.953
ARG727
3.575
ASN728
3.434
CYS729
4.947
MET730
3.648
ALA740
3.750
ASP741
3.345
Ligand Name: 5-[4-(2-chlorophenyl)phenyl]-N-(imidazo[1,2-a]pyridin-6-ylmethyl)-N-methyl-1,3,4-oxadiazol-2-amine Ligand Info
Structure Description MerTK kinase domain with type 1.5 inhibitor from a DNA-encoded library PDB:7AW2
Method X-ray diffraction Resolution 2.10 Å Mutation Yes [3]
PDB Sequence
SHMEELQNKL
577
EDVVIDRNLL
587
ILGRILGEFG
599
SVMEGNLKQE
609
DGTSLKVAVK
619

TMKNSSQREI
631
EEFLSEAACM
641
KDFSHPNVIR
651
LLGVCIEMSS
661
PKPMVILPFM
674

KYGDLHTYLL
684
YSRLETGPRH
694
IPLQTLLRFM
704
VDIALGMEYL
714
SNRNFLHRDL
724

AARNCMLRDD
734
MTVCVADFGL
744
PVKWIAIESL
772
ADRVYTSKSD
782
VWAFGVTMWE
792

IATRGMTPYP
802
GVQNHEMYDY
812
LLHGHRLKQP
822
EDCLDELYEI
832
MYSCWRTDPL
842

DRPTFSVLRL
852
QLERLLESLP
862
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S4W or .S4W2 or .S4W3 or :3S4W;style chemicals stick;color identity;select .A:593 or .A:601 or .A:617 or .A:619 or .A:621 or .A:634 or .A:637 or .A:638 or .A:641 or .A:650 or .A:652 or .A:655 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:730 or .A:740 or .A:741 or .A:742 or .A:744; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
4.241
VAL601
3.917
ALA617
3.422
LYS619
4.023
MET621
3.672
PHE634
3.822
GLU637
3.494
ALA638
3.798
MET641
3.458
ILE650
3.743
LEU652
3.605
Residue
Distance (Å)
VAL655
4.484
VAL669
3.914
LEU671
3.347
PRO672
3.454
PHE673
3.601
MET674
2.868
MET730
3.603
ALA740
3.629
ASP741
2.943
PHE742
3.757
LEU744
3.908
Ligand Name: 4-[4-[5-[Imidazo[1,2-a]pyridin-6-ylmethyl(methyl)amino]-1,3,4-oxadiazol-2-yl]-3-methylphenyl]-2,5-dimethylpyrazole-3-carbonitrile Ligand Info
Structure Description MerTK kinase domain with type 1.5 inhibitor containing a di-methyl, cyano pyrazole group PDB:7OLV
Method X-ray diffraction Resolution 2.13 Å Mutation Yes [13]
PDB Sequence
GSHMEELQNK
576
LEDVVIDRNL
586
LILGRILGEG
596
EFGSVMEGNL
606
KQEDGTSLKV
616

AVKTMSSQRE
630
IEEFLSEAAC
640
MKDFSHPNVI
650
RLLGVCIEMS
660
SQGIPKPMVI
670

LPFMKYGDLH
680
TYLLYSRLET
690
GPRHIPLQTL
700
LRFMVDIALG
710
MEYLSNRNFL
720

HRDLAARNCM
730
LRDDMTVCVA
740
DFGPVKWIAI
769
ESLADRVYTS
779
KSDVWAFGVT
789

MWEIATRGMT
799
PYPGVQNHEM
809
YDYLLHGHRL
819
KQPEDCLDEL
829
YEIMYSCWRT
839

DPLDRPTFSV
849
LRLQLERLLE
859
SLP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .VK2 or .VK22 or .VK23 or :3VK2;style chemicals stick;color identity;select .A:593 or .A:601 or .A:617 or .A:619 or .A:621 or .A:634 or .A:637 or .A:638 or .A:641 or .A:650 or .A:652 or .A:655 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:730 or .A:740 or .A:741 or .A:742 or .A:743; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
4.575
VAL601
3.740
ALA617
3.457
LYS619
4.223
MET621
4.112
PHE634
3.160
GLU637
3.569
ALA638
3.318
MET641
3.607
ILE650
3.814
LEU652
3.252
Residue
Distance (Å)
VAL655
3.657
VAL669
3.850
LEU671
3.276
PRO672
3.451
PHE673
3.573
MET674
2.822
MET730
3.276
ALA740
3.508
ASP741
2.865
PHE742
3.268
GLY743
4.626
Ligand Name: 2-azanyl-~{N}-[(1~{S},2~{S})-2-[[4-[4-[(4-methylpiperazin-1-yl)methyl]phenyl]phenyl]methoxy]cyclopentyl]-5-(1-methylpyrazol-4-yl)pyridine-3-carboxamide Ligand Info
Structure Description Crystal structure of MerTK in complex with a type 1.5 aminopyridine inhibitor PDB:7AAZ
Method X-ray diffraction Resolution 1.85 Å Mutation No [1]
PDB Sequence
QNKLEDVVID
583
RNLLILGKIL
593
GEGEFGSVME
603
GNLKQEDGTS
613
LKVAVKTMKL
623

DNSSQREIEE
633
FLSEAACMKD
643
FSHPNVIRLL
653
GVCIEMSSQG
663
IPKPMVILPF
673

MKYGDLHTYL
683
LYSRLETGPK
693
HIPLQTLLKF
703
MVDIALGMEY
713
LSNRNFLHRD
723

LAARNCMLRD
733
DMTVCVADFG
743
LSKKIYSGDY
753
YRQGRIAKMP
763
VKWIAIESLA
773

DRVYTSKSDV
783
WAFGVTMWEI
793
ATRGMTPYPG
803
VQNHEMYDYL
813
LHGHRLKQPE
823

DCLDELYEIM
833
YSCWRTDPLD
843
RPTFSVLRLQ
853
LEKLLESLPD
863
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .R6K or .R6K2 or .R6K3 or :3R6K;style chemicals stick;color identity;select .A:593 or .A:601 or .A:617 or .A:619 or .A:621 or .A:634 or .A:637 or .A:638 or .A:641 or .A:650 or .A:652 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:727 or .A:728 or .A:730 or .A:740 or .A:741 or .A:742 or .A:743 or .A:744 or .A:745 or .A:746 or .A:753 or .A:754; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.687
VAL601
3.777
ALA617
3.351
LYS619
3.645
MET621
3.609
PHE634
3.611
GLU637
2.558
ALA638
4.534
MET641
3.472
ILE650
3.973
LEU652
3.867
VAL669
3.958
LEU671
3.413
PRO672
2.993
PHE673
3.649
MET674
2.756
Residue
Distance (Å)
LYS675
4.229
TYR676
4.812
GLY677
3.534
ARG727
3.792
ASN728
3.603
MET730
3.506
ALA740
3.694
ASP741
3.097
PHE742
3.409
GLY743
3.498
LEU744
4.352
SER745
3.132
LYS746
4.900
TYR753
3.744
TYR754
4.229
Ligand Name: N-(2-(2-cyclopropylethoxy)pyrimidin-5-yl)-7-methoxy-6-(piperidin-4-ylmethoxy)quinazolin-4-amine Ligand Info
Structure Description MerTK kinase domain in complex with quinazoline-based inhbitor PDB:7AVY
Method X-ray diffraction Resolution 2.31 Å Mutation No [3]
PDB Sequence
KLEDVVIDRN
585
LLILGKILGE
595
GEFGSVMEGN
605
LKQDGTSLKV
616
AVKTMKLDNS
626

SQREIEEFLS
636
EAACMKDFSH
646
PNVIRLLGVC
656
IEMSSQGIPK
666
PMVILPFMKY
676

GDLHTYLLYS
686
RLETGPKHIP
696
LQTLLKFMVD
706
IALGMEYLSN
716
RNFLHRDLAA
726

RNCMLRDDMT
736
VCVADFGLSP
763
VKWIAIESLA
773
DRVYTSKSDV
783
WAFGVTMWEI
793

ATRGMTPYPG
803
VQNHEMYDYL
813
LHGHRLKQPE
823
DCLDELYEIM
833
YSCWRTDPLD
843

RPTFSVLRLQ
853
LEKLLESLPD
863
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .S4E or .S4E2 or .S4E3 or :3S4E;style chemicals stick;color identity;select .A:593 or .A:594 or .A:601 or .A:617 or .A:619 or .A:621 or .A:641 or .A:650 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:677 or .A:678 or .A:681 or .A:730 or .A:740 or .A:741 or .A:742 or .A:744; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.401
GLY594
3.920
VAL601
3.954
ALA617
3.232
LYS619
3.757
MET621
4.375
MET641
4.338
ILE650
3.968
VAL669
4.126
LEU671
3.480
PRO672
3.360
Residue
Distance (Å)
PHE673
3.894
MET674
2.894
LYS675
4.340
GLY677
4.064
ASP678
3.919
THR681
3.960
MET730
3.321
ALA740
3.447
ASP741
3.289
PHE742
3.344
LEU744
3.854
Ligand Name: 3-[4-[6-chloranyl-5-[[(3R)-pyrrolidin-3-yl]amino]-1H-indazol-3-yl]pyrazol-1-yl]benzenecarbonitrile Ligand Info
Structure Description Fragment-based Lead Discovery of Indazole-based Compounds as AXL Kinase Inhibitors PDB:7DXL
Method X-ray diffraction Resolution 3.15 Å Mutation Yes [14]
PDB Sequence
NKLEDVVIDR
584
NLLILGKILG
594
EGEFGSVMEG
604
NLKQEDGTSL
614
KVAVKTMSSQ
628

REIEEFLSEA
638
ACMKDFSHPN
648
VMRLLGVCIE
658
KPMVILPFMK
675
YGDLHTYLLY
685

SRLETGPKHI
695
PLQTLLKFMV
705
DIALGMEYLS
715
NRNFLHRDLA
725
ARNCMLRDDM
735

TVCVADFGLM
762
PVKWIAIESL
772
ADRVYTSKSD
782
VWAFGVTMWE
792
IATRGMTPYP
802

GVQNHEMYDY
812
LLHGHRLKQP
822
EDCLDELYEI
832
MYSCWRTDPL
842
DRPTFSVLRL
852

QLEKLLESLP
862
D
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .E56 or .E562 or .E563 or :3E56;style chemicals stick;color identity;select .A:593 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:727 or .A:728 or .A:730 or .A:740 or .A:741; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.848
VAL601
4.059
ALA617
3.313
LYS619
4.473
MET650
3.491
LEU671
3.744
PRO672
2.560
PHE673
3.684
MET674
3.146
Residue
Distance (Å)
LYS675
3.153
TYR676
4.777
GLY677
3.845
ARG727
3.502
ASN728
3.584
MET730
3.707
ALA740
3.800
ASP741
2.840
Ligand Name: N-[2-{4-[(2s)-4-(Methylsulfonyl)morpholin-2-Yl]-1,3-Thiazol-2-Yl}-4-(Morpholin-4-Yl)phenyl]-1h-Imidazole-2-Carboxamide Ligand Info
Structure Description Structure-based optimization of 1H-imidazole-2-carboxamides as Axl kinase inhibitors utilizing a Mer mutant surrogate PDB:5TD2
Method X-ray diffraction Resolution 2.68 Å Mutation No [7]
PDB Sequence
LEDVVIDRNL
586
LILGKILGEG
596
EFGSVMEGNL
606
KQEDGTSLKV
616
AVKTMAACMK
642

DFSHPNVMRL
652
LGVCIEMSSP
667
MVILPFMKYG
677
DLHTYLLYSR
687
LETGPKHIPL
697

QTLLKFMVDI
707
ALGMEYLSNR
717
NFLHRDLAAR
727
NCMLRDDMTV
737
CVADFPVKWI
767

AIESLYTSKS
781
DVWAFGVTMW
791
EIATRGMTPY
801
PGVQNHEMYD
811
YLLHGHRLKQ
821

PEDCLDELYE
831
IMYSCWRTDP
841
LDRPTFSVLR
851
LQLEKLLESL
861
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .7AE or .7AE2 or .7AE3 or :37AE;style chemicals stick;color identity;select .A:593 or .A:594 or .A:595 or .A:596 or .A:601 or .A:617 or .A:619 or .A:650 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:727 or .A:728 or .A:729 or .A:730 or .A:740 or .A:741; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LEU593
3.878
GLY594
4.210
GLU595
3.594
GLY596
3.596
VAL601
3.759
ALA617
3.346
LYS619
3.114
MET650
3.401
LEU671
3.458
PRO672
3.031
PHE673
3.644
Residue
Distance (Å)
MET674
2.772
LYS675
2.969
TYR676
4.197
GLY677
3.771
ASP678
3.728
ARG727
3.980
ASN728
3.615
CYS729
4.890
MET730
3.502
ALA740
3.736
ASP741
3.457
Ligand Name: cis-4-[(2-[(4-{[4-(1,3-dioxolan-2-yl)pyridin-2-yl]ethynyl}phenyl)amino]-5-{4-[(4-methylpiperazin-1-yl)methyl]phenyl}pyrimidin-4-yl)amino]cyclohexan-1-ol Ligand Info
Structure Description Crystal structure of the catalytic domain of the proto-oncogene tyrosine-protein kinase MER in complex with inhibitor UNC3437 PDB:6MEP
Method X-ray diffraction Resolution 2.89 Å Mutation No [15]
PDB Sequence
KLEDVVIDRN
585
LLILGKILGE
595
GEFGSVMEGN
605
LKQEDGTSLK
615
VAVKTEFLSE
637

AACMKDFSHP
647
NVIRLLGVCI
657
PMVILPFMKY
676
GDLHTYLLYS
686
RLETGPKHIP
696

LQTLLKFMVD
706
IALGMEYLSN
716
RNFLHRDLAA
726
RNCMLRDDMT
736
VCVADFGLSP
763

VKWIAIESLA
773
DRVYTSKSDV
783
WAFGVTMWEI
793
ATRGMTPYPG
803
VQNHEMYDYL
813

LHGHRLKQPE
823
DCLDELYEIM
833
YSCWRTDPLD
843
RPTFSVLRLQ
853
LEKLLESLPD
863
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .9VS or .9VS2 or .9VS3 or :39VS;style chemicals stick;color identity;select .A:591 or .A:593 or .A:594 or .A:595 or .A:601 or .A:603 or .A:617 or .A:619 or .A:641 or .A:644 or .A:649 or .A:650 or .A:651 or .A:652 or .A:669 or .A:671 or .A:672 or .A:673 or .A:674 or .A:675 or .A:676 or .A:677 or .A:678 or .A:681 or .A:727 or .A:730 or .A:740 or .A:741 or .A:742 or .A:743 or .A:744; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS591
2.254
LEU593
2.035
GLY594
3.556
GLU595
4.185
VAL601
2.967
GLU603
4.920
ALA617
3.161
LYS619
2.088
MET641
2.528
PHE644
4.149
VAL649
4.651
ILE650
2.511
ARG651
4.394
LEU652
1.881
VAL669
3.449
LEU671
1.995
Residue
Distance (Å)
PRO672
2.853
PHE673
2.587
MET674
2.247
LYS675
2.813
TYR676
3.935
GLY677
2.862
ASP678
2.302
THR681
3.798
ARG727
4.244
MET730
2.296
ALA740
2.258
ASP741
2.542
PHE742
2.460
GLY743
3.011
LEU744
2.255
References  Top
REF 1 A-loop interactions in Mer tyrosine kinase give rise to inhibitors with two-step mechanism and long residence time of binding. Biochem J. 2020 Nov 27;477(22):4443-4452.
REF 2 Crystal Structure of the Kinase Domain of MerTK in Complex with AZD7762 Provides Clues for Structure-Based Drug Development. Int J Mol Sci. 2020 Oct 23;21(21):7878.
REF 3 Generating Selective Leads for Mer Kinase Inhibitors-Example of a Comprehensive Lead-Generation Strategy. J Med Chem. 2021 Mar 25;64(6):3165-3184.
REF 4 Structural insights into the inhibited states of the Mer receptor tyrosine kinase. J Struct Biol. 2009 Feb;165(2):88-96.
REF 5 Discovery of Novel Small Molecule Mer Kinase Inhibitors for the Treatment of Pediatric Acute Lymphoblastic Leukemia. ACS Med Chem Lett. 2012 Feb 9;3(2):129-134.
REF 6 The Axl kinase domain in complex with a macrocyclic inhibitor offers first structural insights into an active TAM receptor kinase. J Biol Chem. 2017 Sep 22;292(38):15705-15716.
REF 7 Structure-based optimization of 1H-imidazole-2-carboxamides as Axl kinase inhibitors utilizing a Mer mutant surrogate. Bioorg Med Chem Lett. 2017 Feb 15;27(4):1099-1104.
REF 8 Discovery of Macrocyclic Pyrimidines as MerTK-Specific Inhibitors. ChemMedChem. 2017 Feb 3;12(3):207-213.
REF 9 Discovery of Mer specific tyrosine kinase inhibitors for the treatment and prevention of thrombosis. J Med Chem. 2013 Dec 12;56(23):9693-700.
REF 10 Design and Synthesis of Novel Macrocyclic Mer Tyrosine Kinase Inhibitors. ACS Med Chem Lett. 2016 Sep 13;7(12):1044-1049.
REF 11 Pseudo-cyclization through intramolecular hydrogen bond enables discovery of pyridine substituted pyrimidines as new Mer kinase inhibitors. J Med Chem. 2013 Dec 12;56(23):9683-92.
REF 12 Development of [(18)F]MIPS15692, a radiotracer with in?vitro proof-of-concept for the imaging of MER tyrosine kinase (MERTK) in neuroinflammatory disease. Eur J Med Chem. 2021 Dec 15;226:113822.
REF 13 Optimization of an Imidazo[1,2-a]pyridine Series to Afford Highly Selective Type I1/2 Dual Mer/Axl Kinase Inhibitors with In Vivo Efficacy. J Med Chem. 2021 Sep 23;64(18):13524-13539.
REF 14 Fragment-based lead discovery of indazole-based compounds as AXL kinase inhibitors. Bioorg Med Chem. 2021 Nov 1;49:116437.
REF 15 Data-Driven Construction of Antitumor Agents with Controlled Polypharmacology. J Am Chem Soc. 2019 Oct 2;141(39):15700-15709.

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