2WML

Crystal Structure of a Mammalian Sialyltransferase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008373	molecular_function	sialyltransferase activity
A	0009101	biological_process	glycoprotein biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1344

Chain	Residue
A	GLY149
A	ASN150
A	GLY291
A	PHE292
A	GLY293
A	HOH2087

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 1345

Chain	Residue
A	ARG268
A	ASN335
A	HOH2212
A	HOH2213
A	ARG66
A	ARG106
A	ARG109

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19820709","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 340

Chain	Residue	Details
A	ASP285	hydrogen bond acceptor, steric role
A	ASN335	activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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