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 N-[3-({4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl}amino)-4-methoxyphenyl]propanamide Ligand Info
Canonical SMILES CCC(=O)NC1=CC(=C(C=C1)OC)NC2=NC=CC(=C2)C3=C(NC(=N3)SC)C4=CC=C(C=C4)F
InChI 1S/C25H24FN5O2S/c1-4-22(32)28-18-9-10-20(33-2)19(14-18)29-21-13-16(11-12-27-21)24-23(30-25(31-24)34-3)15-5-7-17(26)8-6-15/h5-14H,4H2,1-3H3,(H,27,29)(H,28,32)(H,30,31)
InChIKey MALZDUNFVXBWQG-UHFFFAOYSA-N
PubChem Compound ID 137654533
Drug Binding Sites of Target  Top
PDB ID: 6V6K      EGFR(T790M/V948R) in complex with LN2057
Method X-ray diffraction Resolution 2.20 Å Mutation Yes [1]
PDB Sequence
QALLRILKET
710
EFKKIKVLGS
720
GAFGTVYKGL
730
WIPEGEKVKI
740
PVAIKELREA
750

TSPKANKEIL
760
DEAYVMASVD
770
NPHVCRLLGI
780
CLTSTVQLIM
790
QLMPFGCLLD
800

YVREHKDNIG
810
SQYLLNWCVQ
820
IAKGMNYLED
830
RRLVHRDLAA
840
RNVLVKTPQH
850

VKITDFGLAK
860
LLGAEEKEYH
870
AEGGKVPIKW
880
MALESILHRI
890
YTHQSDVWSY
900

GVTVWELMTF
910
GSKPYDGIPA
920
SEISSILEKG
930
ERLPQPPICT
940
IDVYMIMRKC
950

WMIDADSRPK
960
FRELIIEFSK
970
MARDPQRYLV
980
IQGDERMHLP
990
SPTDSNFYRA
1000

LMDEEDMDDV
1010
VDAD
Residue
Distance (Å)
LEU718
3.214
VAL726
3.408
ALA743
3.379
ILE744
4.118
LYS745
3.000
LEU777
3.896
LEU788
2.990
ILE789
3.200
MET790
3.205
GLN791
3.166
LEU792
3.769
MET793
2.978
Residue
Distance (Å)
PRO794
3.337
PHE795
4.472
GLY796
3.408
CYS797
1.677
LEU798
4.928
LEU799
4.993
ASP800
3.618
ARG841
3.094
ASN842
2.948
LEU844
3.339
THR854
3.735
ASP855
2.923
PDB ID: 6VHN      Wild type EGFR in complex with LN2057
Method X-ray diffraction Resolution 2.40 Å Mutation No [1]
PDB Sequence
GEAPNQALLR
705
ILKETEFKKI
715
KVLGSGAFGT
725
VYKGLWIPEG
735
EKVKIPVAIK
745

ESPKANKEIL
760
DEAYVMASVD
770
NPHVCRLLGI
780
CLTSTVQLIT
790
QLMPFGCLLD
800

YVREHKDNIG
810
SQYLLNWCVQ
820
IAKGMNYLED
830
RRLVHRDLAA
840
RNVLVKTPQH
850

VKITDFGLAK
860
LLVPIKWMAL
883
ESILHRIYTH
893
QSDVWSYGVT
903
VWELMTFGSK
913

PYDGIPASEI
923
SSILEKGERL
933
PQPPICTIDV
943
YMIMVKCWMI
953
DADSRPKFRE
963

LIIEFSKMAR
973
DPQRYLVIQG
983
DEDMDDVVDA
1013
DEYLIP
Residue
Distance (Å)
LEU718
3.544
PHE723
3.627
VAL726
3.619
ALA743
3.407
ILE744
4.483
LYS745
3.403
GLU762
3.868
MET766
4.038
LEU777
3.832
LEU788
3.048
Residue
Distance (Å)
ILE789
3.427
THR790
3.269
GLN791
3.439
LEU792
3.591
MET793
3.081
PRO794
3.433
PHE795
4.657
GLY796
3.759
CYS797
4.056
LEU844
3.614
References  Top
REF 1 Structural Basis for EGFR Mutant Inhibition by Trisubstituted Imidazole Inhibitors. J Med Chem. 2020 Apr 23;63(8):4293-4305.

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