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4UEG

Crystal structure of human glycogenin-2 catalytic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
B0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 1266
ChainResidue
BASP104
BASP106
BHIS214

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1270
ChainResidue
AASP104
AASP106
AHIS214
AHOH2074
AHOH2117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P46976","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P13280","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P13280","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Glc...) tyrosine","evidences":[{"source":"PubMed","id":"9857012","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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