Structure of PDB 5ayy Chain C

Receptor sequence
>5ayyC (length=289) Species: 9606 (Homo sapiens) [Search protein sequence]
MDAEGLALLLPPVTLAALVDSWLREDCPGLNYAALVSGAGPSQAALWAKS
PGVLAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAHCLLLG
ERVALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKY
GLLVGGAASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFALKVEV
ECSSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGG
ITLDNLPQFCGPHIDVISMGMLTQAAPALDFSLKLFAKE
3D structure
PDB5ayy Structural Insights into the Quaternary Catalytic Mechanism of Hexameric Human Quinolinate Phosphoribosyltransferase, a Key Enzyme in de novo NAD Biosynthesis
ChainC
Resolution3.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R102 K139 K171 E201 D222
Catalytic site (residue number reindexed from 1) R102 K139 K171 E201 D222
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 NTM C T137 R138 H160 R161 M169 K171 S268 T137 R138 H160 R161 M169 K171 S268
Gene Ontology
Molecular Function
GO:0004514 nicotinate-nucleotide diphosphorylase (carboxylating) activity
GO:0005515 protein binding
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0042802 identical protein binding
Biological Process
GO:0009435 NAD biosynthetic process
GO:0019363 pyridine nucleotide biosynthetic process
GO:0019674 NAD metabolic process
GO:0034213 quinolinate catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome
GO:1902494 catalytic complex

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Cellular Component
External links
PDB RCSB:5ayy, PDBe:5ayy, PDBj:5ayy
PDBsum5ayy
PubMed26805589
UniProtQ15274|NADC_HUMAN Nicotinate-nucleotide pyrophosphorylase [carboxylating] (Gene Name=QPRT)

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