2FYB

Crystal structure of the catalytic domain of the human beta1,4-galactosyltransferase mutant M339H in complex with Mn and UDP-galactose in open conformation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005975	biological_process	carbohydrate metabolic process
A	0016757	molecular_function	glycosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 402

Chain	Residue
A	ASP250
A	HIS340
A	HIS343
A	UDP403
A	HOH561
A	HOH699

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE UDP A 403

Chain	Residue
A	ARG187
A	PHE222
A	ASP248
A	VAL249
A	ASP250
A	HIS343
A	MN402
A	HOH561
A	HOH652
A	HOH666
A	HOH788
A	PRO183
A	PHE184
A	ARG185

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16497331","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16157350","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19106107","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1fr8

Chain	Residue	Details
A	GLU313
A	ASP315
A	ARG355

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