Structure of PDB 4kww Chain E

Receptor sequence
>4kwwE (length=284) Species: 9606 (Homo sapiens) [Search protein sequence]
AEGLALLLPPVTLAALVDSWLREDCPGLNYAALVSGAGPSQAALWAKSPG
VLAGQPFFDAIFTQLNCQVSWFLPEGSKLVPVARVAEVRGPAHCLLLGER
VALNTLARCSGIASAAAAAVEAARGAGWTGHVAGTRKTTPGFRLVEKYGL
LVGGAASHRYDLGGLVMVKDNHVVAAGGVEKAVRAARQAADFTLKVEVEC
SSLQEAVQAAEAGADLVLLDNFKPEELHPTATVLKAQFPSVAVEASGGIT
LDNLPQFCGPHIDVISMGMLTQAAPALDFSLKLF
3D structure
PDB4kww The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid.
ChainE
Resolution2.55 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) R100 K137 K169 E199 D220
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 E T137 R138 H160 R161 M169 K171 T135 R136 H158 R159 M167 K169
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:4kww, PDBe:4kww, PDBj:4kww
PDBsum4kww
PubMed24038671
UniProtQ15274|NADC_HUMAN Nicotinate-nucleotide pyrophosphorylase [carboxylating] (Gene Name=QPRT)

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