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2XVD

ephB4 kinase domain inhibitor complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AS6 A 1889
ChainResidue
AILE621
AGLU697
AGLY699
ALEU747
ASER757
AASP758
AGLY622
AVAL629
AALA645
AGLU664
AMET668
ATHR693
AGLU694
AMET696

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1890
ChainResidue
AASP740
AASP758
AMG1892
AHOH2095
AHOH2110
AHOH2112
AHOH2113

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1891
ChainResidue
AGLU672
AHOH2039
AHOH2040

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1892
ChainResidue
AASP740
AASP758
AMG1890
AHOH2092
AHOH2110

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGEFGEVCrGrlkapgkkesc.......VAIK
ChainResidueDetails
AILE621-LYS647

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLAARNILV
ChainResidueDetails
ATYR736-VAL748

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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