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6BSU

Crystal structure of xyloglucan xylosyltransferase I

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0016757molecular_functionglycosyltransferase activity
B0016020cellular_componentmembrane
B0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 501
ChainResidue
AASP227
AASP229
AHIS377
AHOH602
AHOH780
AHOH819

site_idAC2
Number of Residues5
Detailsbinding site for residue MN B 501
ChainResidue
BHOH818
BHOH860
BASP227
BASP229
BHIS377

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29784804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BSV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29784804","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BSW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29784804","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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