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5IUS

Crystal structure of human PD-L1 in complex with high affinity PD-1 mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0050777biological_processnegative regulation of immune response
B0016020cellular_componentmembrane
B0050777biological_processnegative regulation of immune response
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsRegion: {"description":"Interaction with CD274/PDCD1L1","evidences":[{"source":"PubMed","id":"26602187","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"28165004","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"28165004","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WT9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues216
DetailsDomain: {"description":"Ig-like V-type"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues184
DetailsDomain: {"description":"Ig-like C2-type"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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