Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T59328 Target Info
Target Name Epidermal growth factor receptor (EGFR)
Synonyms Receptor tyrosine-protein kinase erbB-1; Proto-oncogene c-ErbB-1; HER1; ERBB1; ERBB
Target Type Successful Target
Gene Name EGFR
Biochemical Class Kinase
UniProt ID
EGFR_HUMAN
Ligand General Information  Top
Ligand Name (20R)-10,15,20-trimethyl-2-[(4-methylpiperazin-1-yl)methyl]-18,19,20,21-tetrahydro-15H,17H-12,8-(metheno)pyrazolo[3',4':2,3][1,5,10,12]oxatriazacycloheptadecino[12,11-a]benzimidazol-7(6H)-one Ligand Info
Canonical SMILES CC1CCCOC2=C(C=NN2C)C3=NC(=CC(=C3)C(=O)NC4=NC5=C(N4C1)C=C(C=C5)CN6CCN(CC6)C)C
InChI 1S/C30H38N8O2/c1-20-6-5-13-40-29-24(17-31-36(29)4)26-16-23(14-21(2)32-26)28(39)34-30-33-25-8-7-22(15-27(25)38(30)18-20)19-37-11-9-35(3)10-12-37/h7-8,14-17,20H,5-6,9-13,18-19H2,1-4H3,(H,33,34,39)/t20-/m1/s1
InChIKey AIQBYZOTCIQTGW-HXUWFJFHSA-N
PubChem Compound ID 139600318
Drug Binding Sites of Target  Top
PDB ID: 7KXZ      Active conformation of EGFR kinase in complex with BI-4020
Method X-ray diffraction Resolution 2.40 Å Mutation No [1]
PDB Sequence
GEAPNQALLR
705
ILKETEFKKI
715
KVLGSGAFGT
725
VYKGLWIPEG
735
EKVKIPVAIK
745

ELSPKANKEI
759
LDEAYVMASV
769
DNPHVCRLLG
779
ICLTSTVQLI
789
TQLMPFGCLL
799

DYVREHKDNI
809
GSQYLLNWCV
819
QIAKGMNYLE
829
DRRLVHRDLA
839
ARNVLVKTPQ
849

HVKITDFGLA
859
KLLGAEEKEY
869
HAEGGKVPIK
879
WMALESILHR
889
IYTHQSDVWS
899

YGVTVWELMT
909
FGSKPYDGIP
919
ASEISSILEK
929
GERLPQPPIC
939
TIDVYMIMVK
949

CWMIDADSRP
959
KFRELIIEFS
969
KMARDPQRYL
979
VIQGDERMMD
1008
DVVDADEYL
Residue
Distance (Å)
LEU718
3.714
GLY719
4.633
PHE723
3.555
VAL726
3.575
ALA743
3.590
LYS745
3.007
GLU762
4.274
MET766
4.867
CYS775
3.286
THR790
2.974
GLN791
3.218
Residue
Distance (Å)
LEU792
3.584
MET793
2.952
PRO794
2.949
PHE795
4.244
GLY796
3.622
CYS797
3.607
ASP800
3.290
GLU804
2.926
LEU844
3.371
THR854
3.083
ASP855
3.543
PDB ID: 7KY0      Inactive conformation of EGFR (T790M/V948R) kinase in complex with BI-4020
Method X-ray diffraction Resolution 3.10 Å Mutation Yes [2]
PDB Sequence
NQALLRILKE
709
TEFKKIKVLG
719
SGAFGTVYKG
729
LWIPEGEKVK
739
IPVAIKELRE
749

ATSPKANKEI
759
LDEAYVMASV
769
DNPHVCRLLG
779
ICLTSTVQLI
789
MQLMPFGCLL
799

DYVREHKDNI
809
GSQYLLNWCV
819
QIAKGMNYLE
829
DRRLVHRDLA
839
ARNVLVKTPQ
849

HVKITDFGLA
859
KLVPIKWMAL
883
ESILHRIYTH
893
QSDVWSYGVT
903
VWELMTFGSK
913

PYDGIPASEI
923
SSILEKGERL
933
PQPPICTIDV
943
YMIMRKCWMI
953
DADSRPKFRE
963

LIIEFSKMAR
973
DPQRYLVIQG
983
DERMHLPSPT
993
DSNFYRALMD
1003
EEDM
Residue
Distance (Å)
LYS716
3.781
VAL717
4.064
LEU718
3.512
GLY719
4.590
SER720
4.011
GLY721
4.965
VAL726
3.542
ALA743
3.658
LYS745
2.727
CYS775
4.120
MET790
3.389
GLN791
3.269
Residue
Distance (Å)
LEU792
3.279
MET793
2.782
PRO794
3.277
PHE795
4.415
GLY796
3.555
CYS797
3.428
ARG841
4.763
ASN842
3.573
LEU844
3.308
THR854
2.996
ASP855
3.019
References  Top
REF 1 Structural analysis of the macrocyclic inhibitor BI-4020 binding to the active and inactive conformations of EGFR kinase
REF 2 Structural analysis of the macrocyclic inhibitor BI-4020 binding to the active and inactive conformations of EGFR kinase

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