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 T49507 Target Info
Target Name Ephrin type-B receptor 4 (EPHB4)
Synonyms Tyrosine-protein kinase TYRO11; TYRO11; MYK1; Hepatoma transmembrane kinase; HTK
Target Type Clinical trial Target
Gene Name EPHB4
Biochemical Class Kinase
UniProt ID
EPHB4_HUMAN
Ligand General Information  Top
Ligand Name Staurosporine Ligand Info
Canonical SMILES CC12C(C(CC(O1)N3C4=CC=CC=C4C5=C6C(=C7C8=CC=CC=C8N2C7=C53)CNC6=O)NC)OC
InChI 1S/C28H26N4O3/c1-28-26(34-3)17(29-2)12-20(35-28)31-18-10-6-4-8-14(18)22-23-16(13-30-27(23)33)21-15-9-5-7-11-19(15)32(28)25(21)24(22)31/h4-11,17,20,26,29H,12-13H2,1-3H3,(H,30,33)/t17-,20-,26-,28+/m1/s1
InChIKey HKSZLNNOFSGOKW-FYTWVXJKSA-N
PubChem Compound ID 44259
Drug Binding Sites of Target  Top
PDB ID: 2YN8      ephB4 kinase domain inhibitor complex
Method X-ray diffraction Resolution 2.11 Å Mutation Yes [1]
PDB Sequence
KEIDVSYVKI
617
EEVIGAGEFG
627
EVCRGRLKES
642
CVAIKTLKGG
652
YTERQRREFL
662

SEASIMGQFE
672
HPNIIRLEGV
682
VTNSMPVMIL
692
TEFMENGALD
702
SFLRLNDGQF
712

TVIQLVGMLR
722
GIASGMRYLA
732
EMSYVHRDLA
742
ARNILVNSNL
752
VCKVSDFPIR
785

WTAPEAIAFR
795
KFTSASDVWS
805
YGIVMWEVMS
815
FGERPYWDMS
825
NQDVINAIEQ
835

DYRLPPPPDC
845
PTSLHQLMLD
855
CWQKDRNARP
865
RFPQIVSALD
875
KMIRNPASLK
885

IVA
Residue
Distance (Å)
ILE621
3.490
GLY622
3.639
ALA623
3.437
GLY624
4.940
VAL629
3.806
ALA645
3.246
LYS647
3.236
GLU664
3.396
ILE677
4.182
THR693
3.191
GLU694
2.863
Residue
Distance (Å)
PHE695
3.410
MET696
2.731
GLU697
4.785
GLY699
3.518
ALA700
3.736
ARG744
2.869
ASN745
3.929
LEU747
3.361
SER757
3.034
ASP758
3.643
PDB ID: 3ZEW      Crystal structure of EphB4 in complex with staurosporine
Method X-ray diffraction Resolution 2.50 Å Mutation No [2]
PDB Sequence
EIDVSYVKIE
618
EVIGAGEFGE
628
VCRGRLKAPG
638
KKESCVAIKT
648
LTERQRREFL
662

SEASIMGQFE
672
HPNIIRLEGV
682
VTNSMPVMIL
692
TEFMENGALD
702
SFLRLNDGQF
712

TVIQLVGMLR
722
GIASGMRYLA
732
EMSYVHRDLA
742
ARNILVNSNL
752
VCKVSDFGLS
762

RFLSSDPTTS
776
SKIPIRWTAP
789
EAIAFRKFTS
799
ASDAWSYGIV
809
MWEVMSFGER
819

PYWDMSNQDV
829
INAIEQDYRL
839
PPPPDCPTSL
849
HQLMLDCWQK
859
DRNARPRFPQ
869

VVSALDKMIR
879
NPASLKIVA
Residue
Distance (Å)
ILE621
3.324
GLY622
3.321
ALA623
4.059
GLY624
4.224
VAL629
3.709
ALA645
3.221
LYS647
3.657
GLU664
3.512
ILE677
3.803
THR693
3.349
GLU694
2.945
Residue
Distance (Å)
PHE695
3.334
MET696
2.760
ASN698
4.788
GLY699
3.453
ALA700
3.968
ARG744
2.953
ASN745
3.790
LEU747
3.458
SER757
3.283
ASP758
3.709
References  Top
REF 1 Stability and solubility engineering of the EphB4 tyrosine kinase catalytic domain using a rationally designed synthetic library. Protein Eng Des Sel. 2013 Oct;26(10):695-704.
REF 2 Completing the structural family portrait of the human EphB tyrosine kinase domains. Protein Sci. 2014 May;23(5):627-38.

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