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2QQL

Neuropilin-2 a1a2b1b2 Domains in Complex with a Semaphorin-Blocking Fab

Functional Information from GO Data
ChainGOidnamespacecontents
L0002250biological_processadaptive immune response
L0002376biological_processimmune system process
L0003823molecular_functionantigen binding
L0005576cellular_componentextracellular region
L0005615cellular_componentextracellular space
L0005886cellular_componentplasma membrane
L0006955biological_processimmune response
L0016064biological_processimmunoglobulin mediated immune response
L0019814cellular_componentimmunoglobulin complex
L0050853biological_processB cell receptor signaling pathway
L0070062cellular_componentextracellular exosome
L0071735cellular_componentIgG immunoglobulin complex
L0071738cellular_componentIgD immunoglobulin complex
L0071742cellular_componentIgE immunoglobulin complex
L0071745cellular_componentIgA immunoglobulin complex
L0071753cellular_componentIgM immunoglobulin complex
L0072562cellular_componentblood microparticle
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR192-HIS198
HTYR194-HIS200

site_idPS01285
Number of Residues30
DetailsFA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. GWtpnldsnke......YLqVDlrfltmLtaIaTQG
ChainResidueDetails
AGLY317-GLY346
AGLY473-GLY505

site_idPS01286
Number of Residues17
DetailsFA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Pqtwhsgia..LRlELfGC
ChainResidueDetails
APRO411-CYS427
APRO575-CYS592

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues114
DetailsDomain: {"description":"CUB 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00059","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues150
DetailsDomain: {"description":"F5/8 type C 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17989695","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QQO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17989695","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QQK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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