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4M4R

Epha4 ectodomain complex with ephrin a5

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
B0016020cellular_componentmembrane
B0046875molecular_functionephrin receptor binding
B0048013biological_processephrin receptor signaling pathway
C0005003molecular_functionephrin receptor activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
C0016020cellular_componentmembrane
D0016020cellular_componentmembrane
D0046875molecular_functionephrin receptor binding
D0048013biological_processephrin receptor signaling pathway
E0005003molecular_functionephrin receptor activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
E0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
E0016020cellular_componentmembrane
F0016020cellular_componentmembrane
F0046875molecular_functionephrin receptor binding
F0048013biological_processephrin receptor signaling pathway
G0005003molecular_functionephrin receptor activity
G0005524molecular_functionATP binding
G0006468biological_processprotein phosphorylation
G0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
G0016020cellular_componentmembrane
H0016020cellular_componentmembrane
H0046875molecular_functionephrin receptor binding
H0048013biological_processephrin receptor signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00790
Number of Residues21
DetailsRECEPTOR_TYR_KIN_V_1 Receptor tyrosine kinase class V signature 1. FqDvGACIALVSVRVfykKCP
ChainResidueDetails
APHE185-PRO205

site_idPS00791
Number of Residues21
DetailsRECEPTOR_TYR_KIN_V_2 Receptor tyrosine kinase class V signature 2. CgaDGEWlv.PIGnClCnaGHE
ChainResidueDetails
ACYS247-GLU267

site_idPS01299
Number of Residues28
DetailsEPHRIN_RBD_1 Ephrin receptor-binding (ephrin RBD) domain signature. KFSeKFQlFTPfslGfEFrpgreYFyiS
ChainResidueDetails
BLYS113-SER140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues716
DetailsDomain: {"description":"Eph LBD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00883","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues444
DetailsDomain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues388
DetailsDomain: {"description":"Fibronectin type-III 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues532
DetailsDomain: {"description":"Ephrin RBD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00884","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17400922","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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