Structure of PDB 3c2r Chain A

Receptor sequence
>3c2rA (length=267) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PVYEHLLPVNGAWRQDVTNWLSEDVPSFDFGGYVVGSDLKEANLYCKQDG
MLCGVPFAQEVFNQCELQVEWLFKEGSFLEPSKNDSGKIVVAKITGPAKN
ILLAERTALNILSRSSGIATASHKIISLARSTGYKGTIAGTRKTTPGLRR
LEKYSMLVGGCDTHRYDLSSMVMLKDNHIWATGSITNAVKNARAVCGFAV
KIEVECLSEDEATEAIEAGADVIMLDNHFLLECSGGLNLLCDDIDIYSTS
SIHQGTPVIDFSLKLAH
3D structure
PDB3c2r Comprehensive X-ray Structural Studies of the Quinolinate Phosphoribosyl Transferase (BNA6) from Saccharomyces cerevisiae.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R107 K144 K176 E206 D227
Catalytic site (residue number reindexed from 1) R106 K143 K175 E205 D226
Enzyme Commision number 2.4.2.19: nicotinate-nucleotide diphosphorylase (carboxylating).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PHT A T142 R143 H165 R166 M174 T141 R142 H164 R165 M173 MOAD: Kd=0.78mM
PDBbind-CN: -logKd/Ki=3.11,Kd=0.78mM
Gene Ontology
Molecular Function
GO:0004514 nicotinate-nucleotide diphosphorylase (carboxylating) activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
Biological Process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0034213 quinolinate catabolic process
GO:0034354 'de novo' NAD biosynthetic process from tryptophan
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:3c2r, PDBe:3c2r, PDBj:3c2r
PDBsum3c2r
PubMed18321072
UniProtP43619|NADC_YEAST Nicotinate-nucleotide pyrophosphorylase [carboxylating] (Gene Name=BNA6)

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