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2FY7

Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in apo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005975biological_processcarbohydrate metabolic process
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGE A 403
ChainResidue
APRO175
AHIS176
ACYS262
APHE263
ASER264
AHOH562
AHOH638
AHOH731

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 404
ChainResidue
AASN158
AGLN203
AHOH701
AHOH780
ALEU136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16497331","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16157350","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19106107","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fr8
ChainResidueDetails
AGLU313
AASP315
AARG355

238895

PDB entries from 2025-07-16

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