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-[5-(4-fluorophenyl)-2-(3-hydroxypropyl)-1H-imidazol-4-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)CCCO)C4=CC=C(C=C4)F
InChI 1S/C27H28FN5O3/c1-3-25(35)30-20-10-11-22(36-2)21(16-20)31-24-15-18(12-13-29-24)27-26(17-6-8-19(28)9-7-17)32-23(33-27)5-4-14-34/h6-13,15-16,34H,3-5,14H2,1-2H3,(H,29,31)(H,30,35)(H,32,33)
InChIKey QQVFPBLJZZDHSS-UHFFFAOYSA-N
PubChem Compound ID 135314117
Drug Binding Sites of Target  Top
PDB ID: 6V6O      EGFR(T790M/V948R) in complex with LN2380
Method X-ray diffraction Resolution 2.10 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
3.547
SER720
4.020
GLY721
4.331
VAL726
3.639
ALA743
3.374
ILE744
3.970
LYS745
2.920
LEU777
3.900
LEU788
2.993
ILE789
3.263
MET790
3.276
GLN791
3.235
Residue
Distance (Å)
LEU792
3.766
MET793
2.801
PRO794
3.608
GLY796
3.413
CYS797
1.766
ASP800
3.122
ARG841
2.483
ASN842
3.859
LEU844
3.321
THR854
3.408
ASP855
3.316
PDB ID: 6VH4      Wild type EGFR in complex with LN2380
Method X-ray diffraction Resolution 2.80 Å Mutation No [1]
PDB Sequence
GEAPNQALLR
705
ILKETEFKKI
715
KVLGSGAFGT
725
VYKGLWIPEG
735
EKVKIPVAIK
745

ELPKANKEIL
760
DEAYVMASVD
770
NPHVCRLLGI
780
CLTSTVQLIT
790
QLMPFGCLLD
800

YVREHKDNIG
810
SQYLLNWCVQ
820
IAKGMNYLED
830
RRLVHRDLAA
840
RNVLVKTPQH
850

VKITDFGLAK
860
LLGAEYHAEG
873
GKVPIKWMAL
883
ESILHRIYTH
893
QSDVWSYGVT
903

VWELMTFGSK
913
PYDGIPASEI
923
SSILEKGERL
933
PQPPICTIDV
943
YMIMVKCWMI
953

DADSRPKFRE
963
LIIEFSKMAR
973
DPQRYLVIQG
983
DDMDDVVDAD
1014
EYLIP
Residue
Distance (Å)
LEU718
3.599
VAL726
3.897
ALA743
3.349
ILE744
4.181
LYS745
3.555
GLU762
4.243
MET766
3.710
LEU777
3.924
LEU788
3.019
ILE789
3.510
THR790
3.502
GLN791
3.159
Residue
Distance (Å)
LEU792
3.684
MET793
2.794
PRO794
3.298
GLY796
3.492
CYS797
1.861
ASP800
3.320
ARG841
3.519
ASN842
3.292
LEU844
3.468
THR854
4.238
ASP855
3.995
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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