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 T57278 Target Info
Target Name Ephrin type-A receptor 2 (EPHA2)
Synonyms Tyrosine-protein kinase receptor ECK; Epithelial cell kinase; EphA2receptor; ECK
Target Type Clinical trial Target
Gene Name EPHA2
Biochemical Class Kinase
UniProt ID
EPHA2_HUMAN
Ligand General Information  Top
Ligand Name AMP-PNP Ligand Info
Canonical SMILES C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
InChI 1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKey PVKSNHVPLWYQGJ-KQYNXXCUSA-N
PubChem Compound ID 33113
Drug Binding Sites of Target  Top
PDB ID: 1MQB      Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase
Method X-ray diffraction Resolution 2.30 Å Mutation No [1]
PDB Sequence
TTEIHPSCVT
614
RQKVIGAGEF
624
GEVYKGMLKT
634
KKEVPVAIKT
647
LKAGYTEKQR
657

VDFLGEAGIM
667
GQFSHHNIIR
677
LEGVISKYKP
687
MMIITEYMEN
697
GALDKFLREK
707

DGEFSVLQLV
717
GMLRGIAAGM
727
KYLANMNYVH
737
RDLAARNILV
747
NSNLVCKVSD
757

FGLKIPIRWT
784
APEAISYRKF
794
TSASDVWSFG
804
IVMWEVMTYG
814
ERPYWELSNH
824

EVMKAINDGF
834
RLPTPMDCPS
844
AIYQLMMQCW
854
QQERARRPKF
864
ADIVSILDKL
874

IRAPDSLKTL
884
ADF
Residue
Distance (Å)
ILE619
3.884
GLY620
3.917
ALA621
3.079
GLY622
3.515
GLU623
3.919
VAL627
3.782
ALA644
3.212
LYS646
3.103
ILE676
4.594
Residue
Distance (Å)
THR692
2.906
GLU693
2.988
TYR694
3.589
MET695
2.982
GLU696
4.953
GLY698
4.347
ALA699
4.320
ASN744
4.620
LEU746
3.686
PDB ID: 5I9W      Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with ANP
Method X-ray diffraction Resolution 1.36 Å Mutation No [2]
PDB Sequence
TTEIHPSCVT
614
RQKVIGAGEF
624
GEVYKGMLKE
640
VPVAIKTLKA
650
GYTEKQRVDF
660

LGEAGIMGQF
670
SHHNIIRLEG
680
VISKYKPMMI
690
ITEYMENGAL
700
DKFLREKDGE
710

FSVLQLVGML
720
RGIAAGMKYL
730
ANMNYVHRDL
740
AARNILVNSN
750
LVCKVSDFGL
760

IPIRWTAPEA
788
ISYRKFTSAS
798
DVWSFGIVMW
808
EVMTYGERPY
818
WELSNHEVMK
828

AINDGFRLPT
838
PMDCPSAIYQ
848
LMMQCWQQER
858
ARRPKFADIV
868
SILDKLIRAP
878

DSLKTLADFD
888
PRVSIRL
Residue
Distance (Å)
ILE619
3.583
GLY620
3.929
ALA621
2.766
GLY622
3.213
GLU623
3.978
VAL627
3.622
ALA644
3.328
LYS646
4.639
ILE676
4.738
THR692
3.537
Residue
Distance (Å)
GLU693
2.870
TYR694
3.536
MET695
2.913
GLY698
4.559
ALA699
3.864
ASN744
4.714
LEU746
3.482
SER756
4.629
ASP757
4.773
References  Top
REF 1 Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. Structure. 2002 Dec;10(12):1659-67.
REF 2 Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs. ACS Chem Biol. 2016 Dec 16;11(12):3400-3411.

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