1FO8

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008375	molecular_function	acetylglucosaminyltransferase activity
A	0009101	biological_process	glycoprotein biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MMC A 1448

Chain	Residue
A	CYS123
A	VAL210
A	GLU211
A	ASP212
A	ASP213
A	LEU214
A	GLU215
A	VAL216
A	PHE316

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11032794","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16769084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FOA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AM5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2APC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11032794","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FOA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP291

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 770

Chain	Residue	Details
A	ASP213	metal ligand
A	ASP291	activator, proton acceptor, proton donor

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