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3CU0

human beta 1,3-glucuronyltransferase I (GlcAT-I) in complex with UDP and GAL-GAL(6-SO4)-XYL(2-PO4)-O-SER

Functional Information from GO Data
ChainGOidnamespacecontents
A0015018molecular_functiongalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
A0016020cellular_componentmembrane
B0015018molecular_functiongalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
B0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsRegion: {"description":"Interaction with galactose moiety of substrate glycoprotein"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues46
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"11950836","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Interaction with galactose moiety of substrate glycoprotein"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kws
ChainResidueDetails
AGLU281

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1kws
ChainResidueDetails
BGLU281

site_idMCSA1
Number of Residues2
DetailsM-CSA 801
ChainResidueDetails
AASP196metal ligand
AGLU281proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 801
ChainResidueDetails
BASP196metal ligand
BGLU281proton acceptor, proton donor

249697

PDB entries from 2026-02-25

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