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6USC

Structure of Human Intelectin-1 in complex with KO

Functional Information from GO Data
ChainGOidnamespacecontents
A0001934biological_processpositive regulation of protein phosphorylation
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0009624biological_processresponse to nematode
A0030246molecular_functioncarbohydrate binding
A0031526cellular_componentbrush border membrane
A0042802molecular_functionidentical protein binding
A0043235cellular_componentreceptor complex
A0045121cellular_componentmembrane raft
A0046326biological_processpositive regulation of D-glucose import
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0070207biological_processprotein homotrimerization
A0070492molecular_functionoligosaccharide binding
A0098552cellular_componentside of membrane
B0001934biological_processpositive regulation of protein phosphorylation
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0009624biological_processresponse to nematode
B0030246molecular_functioncarbohydrate binding
B0031526cellular_componentbrush border membrane
B0042802molecular_functionidentical protein binding
B0043235cellular_componentreceptor complex
B0045121cellular_componentmembrane raft
B0046326biological_processpositive regulation of D-glucose import
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0070207biological_processprotein homotrimerization
B0070492molecular_functionoligosaccharide binding
B0098552cellular_componentside of membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsPropeptide: {"featureId":"PRO_0000009144","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26148048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WMQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26148048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WMY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsLipidation: {"description":"GPI-anchor amidated serine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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