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1SHW

EphB2 / EphrinA5 Complex Structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0046875molecular_functionephrin receptor binding
A0048013biological_processephrin receptor signaling pathway
B0005003molecular_functionephrin receptor activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00790
Number of Residues21
DetailsRECEPTOR_TYR_KIN_V_1 Receptor tyrosine kinase class V signature 1. FqDyGGCMSLIAVRVfyrKCP
ChainResidueDetails
BPHE386-PRO406

site_idPS01299
Number of Residues28
DetailsEPHRIN_RBD_1 Ephrin receptor-binding (ephrin RBD) domain signature. KFSeKFQlFTPfslGfEFrpgreYFyiS
ChainResidueDetails
ALYS117-SER144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues133
DetailsDomain: {"description":"Ephrin RBD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00884","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15107857","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical","evidences":[{"source":"PubMed","id":"19656770","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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