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 N-(2-chloro-6-methylphenyl)-2-[3-[[(3R,4R)-3-fluoropiperidin-4-yl]carbamoyl]anilino]-1,3-thiazole-5-carboxamide Ligand Info
Canonical SMILES CC1=C(C(=CC=C1)Cl)NC(=O)C2=CN=C(S2)NC3=CC=CC(=C3)C(=O)NC4CCNCC4F
InChI 1S/C23H23ClFN5O2S/c1-13-4-2-7-16(24)20(13)30-22(32)19-12-27-23(33-19)28-15-6-3-5-14(10-15)21(31)29-18-8-9-26-11-17(18)25/h2-7,10,12,17-18,26H,8-9,11H2,1H3,(H,27,28)(H,29,31)(H,30,32)/t17-,18-/m1/s1
InChIKey RRUBGRARVNLPQT-QZTJIDSGSA-N
PubChem Compound ID 127053580
Drug Binding Sites of Target  Top
PDB ID: 5NK2      Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with Compound 2b
Method X-ray diffraction Resolution 1.65 Å Mutation No [1]
PDB Sequence
NQAVLKFTTE
607
IHPSCVTRQK
617
VIGAGEFGEV
627
YKGMLKKEVP
642
VAIKTLKAGY
652

TEKQRVDFLG
662
EAGIMGQFSH
672
HNIIRLEGVI
682
SKYKPMMIIT
692
EYMENGALDK
702

FLREKDGEFS
712
VLQLVGMLRG
722
IAAGMKYLAN
732
MNYVHRDLAA
742
RNILVNSNLV
752

CKVSDFGLSR
762
VLEDDPEATY
772
GKIPIRWTAP
786
EAISYRKFTS
796
ASDVWSFGIV
806

MWEVMTYGER
816
PYWELSNHEV
826
MKAINDGFRL
836
PTPMDCPSAI
846
YQLMMQCWQQ
856

ERARRPKFAD
866
IVSILDKLIR
876
APDSLKTLAD
886
FDPRVSIRLP
896
Residue
Distance (Å)
LYS617
4.772
ILE619
3.786
VAL627
3.938
ALA644
3.317
ILE645
3.872
LYS646
3.444
GLU663
3.391
MET667
3.889
ILE676
4.169
ILE690
3.568
ILE691
4.769
THR692
2.942
Residue
Distance (Å)
GLU693
3.505
TYR694
2.557
MET695
2.796
GLU696
3.047
ASN697
3.875
GLY698
3.595
ALA699
4.429
GLU706
4.815
LEU746
3.645
SER756
3.459
ASP757
4.401
PDB ID: 5NK7      Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with Compound 2a
Method X-ray diffraction Resolution 1.89 Å Mutation No [1]
PDB Sequence
FTTEIHPSCV
613
TRQKVIGAGE
623
FGEVYKGMLK
633
KEVPVAIKTL
648
KAGYTEKQRV
658

DFLGEAGIMG
668
QFSHHNIIRL
678
EGVISKYKPM
688
MIITEYMENG
698
ALDKFLREKD
708

GEFSVLQLVG
718
MLRGIAAGMK
728
YLANMNYVHR
738
DLAARNILVN
748
SNLVCKVSDF
758

GLSRVLEDDP
768
EATYGKIPIR
782
WTAPEAISYR
792
KFTSASDVWS
802
FGIVMWEVMT
812

YGERPYWELS
822
NHEVMKAIND
832
GFRLPTPMDC
842
PSAIYQLMMQ
852
CWQQERARRP
862

KFADIVSILD
872
KLIRAPDSLK
882
TLADFDPRVS
892
IRLP
Residue
Distance (Å)
ILE619
3.724
VAL627
3.749
ALA644
3.358
ILE645
3.788
LYS646
3.488
GLU663
3.412
MET667
3.906
ILE676
4.151
ILE690
3.553
ILE691
4.884
THR692
2.942
Residue
Distance (Å)
GLU693
3.555
TYR694
2.692
MET695
2.834
GLU696
3.437
ASN697
4.153
GLY698
3.574
ALA699
4.405
LEU746
3.618
SER756
2.998
ASP757
4.396
References  Top
REF 1 Chemoproteomics-Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors. ChemMedChem. 2017 Jun 21;12(12):999-1011.

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