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 Erlotinib Ligand Info
Canonical SMILES COCCOC1=C(C=C2C(=C1)C(=NC=N2)NC3=CC=CC(=C3)C#C)OCCOC
InChI 1S/C22H23N3O4/c1-4-16-6-5-7-17(12-16)25-22-18-13-20(28-10-8-26-2)21(29-11-9-27-3)14-19(18)23-15-24-22/h1,5-7,12-15H,8-11H2,2-3H3,(H,23,24,25)
InChIKey AAKJLRGGTJKAMG-UHFFFAOYSA-N
PubChem Compound ID 176870
Drug Binding Sites of Target  Top
PDB ID: 4HJO      Crystal structure of the inactive EGFR tyrosine kinase domain with erlotinib
Method X-ray diffraction Resolution 2.75 Å Mutation Yes [1]
PDB Sequence
LLRILKETEF
688
KKIKVLGSGA
698
FGTVYKGLWI
708
PVKIPVAIKE
722
LREATSPKAN
732

KEILDEAYVM
742
ASVDNPHVCR
752
LLGICLTSTV
762
QLITQLMPFG
772
CLLDYVREHK
782

DNIGSQYLLN
792
WCVQIAKGMN
802
YLEDRRLVHR
812
DLAARNVLVK
822
TPQHVKITDF
832

GLAKLLGAEE
842
KEYHAEGGKV
852
PIKWMALESI
862
LHRIYTHQSD
872
VWSYGVTVWE
882

LMTFGSKPYD
892
GIPASEISSI
902
LEKGERLPQP
912
PICTIDVYMI
922
MRKCWMIDAD
932

SRPKFRELII
942
EFSKMARDPQ
952
RYLVIQGD
Residue
Distance (Å)
LEU694
3.702
VAL702
3.697
LYS704
4.863
ALA719
3.339
ILE720
4.275
LYS721
3.484
LEU764
2.890
ILE765
4.088
THR766
3.480
GLN767
3.181
Residue
Distance (Å)
LEU768
3.634
MET769
2.918
PRO770
3.142
PHE771
3.484
GLY772
3.300
CYS773
3.537
ASP776
3.834
LEU820
3.282
THR830
3.668
ASP831
3.177
PDB ID: 1M17      Epidermal Growth Factor Receptor tyrosine kinase domain with 4-anilinoquinazoline inhibitor erlotinib
Method X-ray diffraction Resolution 2.60 Å Mutation No [2]
PDB Sequence
GEAPNQALLR
681
ILKETEFKKI
691
KVLGSGAFGT
701
VYKGLWIPEG
711
EKVKIPVAIK
721

ELREATSPKA
731
NKEILDEAYV
741
MASVDNPHVC
751
RLLGICLTST
761
VQLITQLMPF
771

GCLLDYVREH
781
KDNIGSQYLL
791
NWCVQIAKGM
801
NYLEDRRLVH
811
RDLAARNVLV
821

KTPQHVKITD
831
FGLAKLLGAE
841
EKEYHAEGGK
851
VPIKWMALES
861
ILHRIYTHQS
871

DVWSYGVTVW
881
ELMTFGSKPY
891
DGIPASEISS
901
ILEKGERLPQ
911
PPICTIDVYM
921

IMVKCWMIDA
931
DSRPKFRELI
941
IEFSKMARDP
951
QRYLVIQGDE
961
RMHLMDEEDM
983

DDVVDADEYL
993
IP
Residue
Distance (Å)
LEU694
3.269
GLY695
4.503
VAL702
4.191
ALA719
3.307
LYS721
3.700
GLU738
3.806
MET742
4.632
LEU764
3.431
ILE765
4.451
THR766
3.406
Residue
Distance (Å)
GLN767
3.146
LEU768
3.496
MET769
2.699
PRO770
3.107
PHE771
3.446
GLY772
3.238
CYS773
4.727
LEU820
3.453
THR830
3.652
ASP831
3.105
References  Top
REF 1 Erlotinib binds both inactive and active conformations of the EGFR tyrosine kinase domain. Biochem J. 2012 Dec 15;448(3):417-23.
REF 2 Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J Biol Chem. 2002 Nov 29;277(48):46265-72.

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