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 PD-168393 Ligand Info
Canonical SMILES C=CC(=O)NC1=CC2=C(C=C1)N=CN=C2NC3=CC(=CC=C3)Br
InChI 1S/C17H13BrN4O/c1-2-16(23)21-13-6-7-15-14(9-13)17(20-10-19-15)22-12-5-3-4-11(18)8-12/h2-10H,1H2,(H,21,23)(H,19,20,22)
InChIKey HTUBKQUPEREOGA-UHFFFAOYSA-N
PubChem Compound ID 4708
Drug Binding Sites of Target  Top
PDB ID: 4LQM      EGFR L858R in complex with PD168393
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [1]
PDB Sequence
EAPNQALLRI
706
LKETEFKKIK
716
VLGSGAFGTV
726
YKGLWIPEGE
736
KVKIPVAIKE
746

LTSPKANKEI
759
LDEAYVMASV
769
DNPHVCRLLG
779
ICLTSTVQLI
789
TQLMPFGCLL
799

DYVREHKDNI
809
GSQYLLNWCV
819
QIAKGMNYLE
829
DRRLVHRDLA
839
ARNVLVKTPQ
849

HVKITDFGRA
859
KLLGAEEGKV
876
PIKWMALESI
886
LHRIYTHQSD
896
VWSYGVTVWE
906

LMTFGSKPYD
916
GIPASEISSI
926
LEKGERLPQP
936
PICTIDVYMI
946
MVKCWMIDAD
956

SRPKFRELII
966
EFSKMARDPQ
976
RYLVIQGDER
986
MHLPSALMDE
1004
EDMDDVVDAD
1014

EYLIP
Residue
Distance (Å)
LEU718
3.783
VAL726
4.505
ALA743
3.184
ILE744
4.858
LYS745
3.554
GLU762
3.392
MET766
4.047
LEU777
4.869
LEU788
3.526
ILE789
4.282
THR790
3.355
Residue
Distance (Å)
GLN791
3.399
LEU792
4.064
MET793
3.160
GLY796
3.599
CYS797
1.795
ASP800
3.469
ARG841
3.812
LEU844
3.426
THR854
3.834
ASP855
4.183
PDB ID: 2J5F      Crystal structure of EGFR kinase domain in complex with an irreversible inhibitor 34-jab
Method X-ray diffraction Resolution 3.00 Å Mutation No [2]
PDB Sequence
GEAPNQALLR
705
ILKETEFKKI
715
KVLGSGAFGT
725
VYKGLWIPEG
735
EKVKIPVAIK
745

ELREATSPKA
755
NKEILDEAYV
765
MASVDNPHVC
775
RLLGICLTST
785
VQLITQLMPF
795

GCLLDYVREH
805
KDNIGSQYLL
815
NWCVQIAKGM
825
NYLEDRRLVH
835
RDLAARNVLV
845

KTPQHVKITD
855
FGLAKLLGAE
865
EKVPIKWMAL
883
ESILHRIYTH
893
QSDVWSYGVT
903

VWELMTFGSK
913
PYDGIPASEI
923
SSILEKGERL
933
PQPPICTIDV
943
YMIMVKCWMI
953

DADSRPKFRE
963
LIIEFSKMAR
973
DPQRYLVIQG
983
DERMHLPSPL
1001
MDEEDMDDVV
1011

DADEYLIPQ
Residue
Distance (Å)
LEU718
3.965
VAL726
4.180
ALA743
3.260
ILE744
4.768
LYS745
3.596
GLU762
3.367
MET766
3.816
LEU788
3.101
ILE789
3.800
THR790
3.327
Residue
Distance (Å)
GLN791
3.118
LEU792
3.958
MET793
3.332
GLY796
3.801
CYS797
1.826
ASP800
3.427
ARG841
4.689
LEU844
3.449
THR854
3.811
ASP855
3.859
References  Top
REF 1 Structural, biochemical, and clinical characterization of epidermal growth factor receptor (EGFR) exon 20 insertion mutations in lung cancer. Sci Transl Med. 2013 Dec 18;5(216):216ra177.
REF 2 Structure-guided development of affinity probes for tyrosine kinases using chemical genetics. Nat Chem Biol. 2007 Apr;3(4):229-38.

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