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12HR

structure of human GluD1 with calcium

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues240
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues684
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38060673","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BLJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8BN2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8BN5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"38060673","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BLJ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Essential for dimerization","evidences":[{"source":"UniProtKB","id":"Q61627","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"38060673","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BLJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8BN2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8BN5","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

262513

PDB entries from 2026-11-04

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