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 Dacomitinib Ligand Info
Canonical SMILES COC1=C(C=C2C(=C1)N=CN=C2NC3=CC(=C(C=C3)F)Cl)NC(=O)C=CCN4CCCCC4
InChI 1S/C24H25ClFN5O2/c1-33-22-14-20-17(24(28-15-27-20)29-16-7-8-19(26)18(25)12-16)13-21(22)30-23(32)6-5-11-31-9-3-2-4-10-31/h5-8,12-15H,2-4,9-11H2,1H3,(H,30,32)(H,27,28,29)/b6-5+
InChIKey LVXJQMNHJWSHET-AATRIKPKSA-N
PubChem Compound ID 11511120
Drug Binding Sites of Target  Top
PDB ID: 4I24      Structure of T790M EGFR kinase domain co-crystallized with dacomitinib
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [1]
PDB Sequence
NQALLRILKE
709
TEFKKIKVLG
719
SGAFGTVYKG
729
LWIPEGEKVK
739
IPVAIKELAN
756

KEILDEAYVM
766
ASVDNPHVCR
776
LLGICLTSTV
786
QLIMQLMPFG
796
CLLDYVREHK
806

DNIGSQYLLN
816
WCVQIAKGMN
826
YLEDRRLVHR
836
DLAARNVLVK
846
TPQHVKITDF
856

GLAKLLVPIK
879
WMALESILHR
889
IYTHQSDVWS
899
YGVTVWELMT
909
FGSKPYDGIP
919

ASEISSILEK
929
GERLPQPPIC
939
TIDVYMIMVK
949
CWMIDADSRP
959
KFRELIIEFS
969

KMARDPQRYL
979
VIQGDERMHL
989
PSPTDSNFYR
999
ALMDEEDMDD
1009
VVDAD
Residue
Distance (Å)
LEU718
3.821
VAL726
3.981
ALA743
3.356
ILE744
3.861
LYS745
3.387
LEU788
3.203
ILE789
4.371
MET790
3.407
GLN791
3.178
LEU792
3.740
MET793
2.917
Residue
Distance (Å)
PRO794
3.454
PHE795
4.414
GLY796
3.237
CYS797
1.837
LEU799
4.260
ASP800
3.182
ARG841
4.135
LEU844
3.409
THR854
3.346
ASP855
3.116
LEU858
4.545
PDB ID: 4I23      Crystal structure of the wild-type EGFR kinase domain in complex with dacomitinib (soaked)
Method X-ray diffraction Resolution 2.80 Å Mutation No [1]
PDB Sequence
SGEAPNQALL
704
RILKETEFKK
714
IKVLGSGTVY
727
KGLWIPEGEK
737
VKIPVAIKEL
747

ATSPKANKEI
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
VIQGDERMHL
989
PDMDDVVDAD
1014

EYLI
Residue
Distance (Å)
LEU718
3.596
VAL726
4.280
ALA743
3.453
ILE744
4.556
LYS745
3.632
GLU762
3.498
MET766
3.494
LEU788
3.469
ILE789
4.179
Residue
Distance (Å)
THR790
3.138
GLN791
3.339
LEU792
3.730
MET793
2.749
PRO794
3.620
GLY796
3.477
LEU844
3.837
THR854
3.794
ASP855
4.869
References  Top
REF 1 Insights into the aberrant activity of mutant EGFR kinase domain and drug recognition. Structure. 2013 Feb 5;21(2):209-19.

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