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7S7K

Crystal structure of the EphB2 extracellular domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0005003molecular_functionephrin receptor activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
A0016020cellular_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
APHE178-PRO198

site_idPS00791
Number of Residues21
DetailsRECEPTOR_TYR_KIN_V_2 Receptor tyrosine kinase class V signature 2. CngDGEWlv.PIGrCmCkaGFE
ChainResidueDetails
ACYS241-GLU261

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CmCkaGFeavengtvC
ChainResidueDetails
ACYS254-CYS269

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues524
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues182
DetailsDomain: {"description":"Eph LBD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00883","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues110
DetailsDomain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues95
DetailsDomain: {"description":"Fibronectin type-III 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Cleavage; by a metalloproteinase","evidences":[{"source":"PubMed","id":"17428795","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19656770","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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