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8V9Q

Crystal structure of mGalNAc-T1 in complex with the mucin glycopeptide Muc5AC-13, Mn2+, and UDP.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004653molecular_functionpolypeptide N-acetylgalactosaminyltransferase activity
A0005576cellular_componentextracellular region
A0005794cellular_componentGolgi apparatus
A0006486biological_processprotein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0018242biological_processprotein O-linked glycosylation via serine
A0018243biological_processprotein O-linked glycosylation via threonine
A0030145molecular_functionmanganese ion binding
A0030246molecular_functioncarbohydrate binding
A0032580cellular_componentGolgi cisterna membrane
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
B0004653molecular_functionpolypeptide N-acetylgalactosaminyltransferase activity
B0005576cellular_componentextracellular region
B0005794cellular_componentGolgi apparatus
B0006486biological_processprotein glycosylation
B0006493biological_processprotein O-linked glycosylation
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0018242biological_processprotein O-linked glycosylation via serine
B0018243biological_processprotein O-linked glycosylation via threonine
B0030145molecular_functionmanganese ion binding
B0030246molecular_functioncarbohydrate binding
B0032580cellular_componentGolgi cisterna membrane
B0046872molecular_functionmetal ion binding
B0048471cellular_componentperinuclear region of cytoplasm
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues122
DetailsDomain: {"description":"Ricin B-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00174","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues110
DetailsRegion: {"description":"Catalytic subdomain A","evidences":[{"source":"PubMed","id":"10037781","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues62
DetailsRegion: {"description":"Catalytic subdomain B","evidences":[{"source":"PubMed","id":"10037781","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15486088","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
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":"15486088","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine","evidences":[{"source":"PubMed","id":"25939779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AJO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine","evidences":[{"source":"PubMed","id":"25939779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AJO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AJP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2025-07-23

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