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3BN3

crystal structure of ICAM-5 in complex with aL I domain

Functional Information from GO Data
ChainGOidnamespacecontents
B0005178molecular_functionintegrin binding
B0007155biological_processcell adhesion
B0016020cellular_componentmembrane
B0098609biological_processcell-cell adhesion
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues171
DetailsDomain: {"description":"VWFA","evidences":[{"source":"PROSITE-ProRule","id":"PRU00219","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues82
DetailsDomain: {"description":"Ig-like C2-type 1"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"15144186","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"18691975","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18691975","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2026-01-14

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