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6VXK

Cryo-EM Structure of the full-length A39R/PlexinC1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0030215molecular_functionsemaphorin receptor binding
B0002116cellular_componentsemaphorin receptor complex
B0005102molecular_functionsignaling receptor binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007162biological_processnegative regulation of cell adhesion
B0007416biological_processsynapse assembly
B0008360biological_processregulation of cell shape
B0016020cellular_componentmembrane
B0017154molecular_functionsemaphorin receptor activity
B0030334biological_processregulation of cell migration
B0050772biological_processpositive regulation of axonogenesis
B0071526biological_processsemaphorin-plexin signaling pathway
B0150053cellular_componentcerebellar climbing fiber to Purkinje cell synapse
B1905806biological_processregulation of synapse pruning
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0030215molecular_functionsemaphorin receptor binding
D0002116cellular_componentsemaphorin receptor complex
D0005102molecular_functionsignaling receptor binding
D0005515molecular_functionprotein binding
D0005886cellular_componentplasma membrane
D0007155biological_processcell adhesion
D0007162biological_processnegative regulation of cell adhesion
D0007416biological_processsynapse assembly
D0008360biological_processregulation of cell shape
D0016020cellular_componentmembrane
D0017154molecular_functionsemaphorin receptor activity
D0030334biological_processregulation of cell migration
D0050772biological_processpositive regulation of axonogenesis
D0071526biological_processsemaphorin-plexin signaling pathway
D0150053cellular_componentcerebellar climbing fiber to Purkinje cell synapse
D1905806biological_processregulation of synapse pruning
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. LICNKSFLVtV
ChainResidueDetails
BLEU1059-VAL1069

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20727575","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-04-01

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