1YTD

Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum, Native Structure

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
A	0004516	molecular_function	nicotinate phosphoribosyltransferase activity
A	0009435	biological_process	NAD+ biosynthetic process
A	0016763	molecular_function	pentosyltransferase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15753098","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15753098","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1YTK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of a zinc ion bound nicotinate phosphoribosyltransferase from Thermoplasma acidophilum.","authoringGroup":["Berkeley structural genomics center (BSGC)"]}}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P22253","evidenceCode":"ECO:0000250"}]}

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 1qpr

Chain	Residue	Details
A	THR107

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