Structure of PDB 1qpr Chain D

Receptor sequence
>1qprD (length=284) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
GLSDWELAAARAAIARGLDEDLRYGPDVTTLATVPASATTTASLVTREAG
VVAGLDVALLTLNEVLGTNGYRVLDRVEDGARVPPGEALMTLEAQTRGLL
TAERTMLNLVGHLSGIATATAAWVDAVRGTKAKIRDTRKTLPGLRALQKY
AVRTGGGVNHRLGLGDAALIKDNHVAAAGSVVDALRAVRNAAPDLPCEVE
VDSLEQLDAVLPEKPELILLDNFAVWQTQTAVQRRDSRAPTVMLESSGGL
SLQTAATYAETGVDYLAVGALTHSVRVLDIGLDM
3D structure
PDB1qpr Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target.
ChainD
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R105 K140 K172 E201 D222
Catalytic site (residue number reindexed from 1) R104 K139 K171 E200 D221
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 MN D E201 D222 E200 D221
BS02 PPC D K140 D222 S248 G270 K139 D221 S247 G269
BS03 PHT D T138 R139 H161 R162 L170 K172 T137 R138 H160 R161 L169 K171
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
Cellular Component
GO:0005737 cytoplasm
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall

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Molecular Function
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Cellular Component
External links
PDB RCSB:1qpr, PDBe:1qpr, PDBj:1qpr
PDBsum1qpr
PubMed9862811
UniProtP9WJJ7|NADC_MYCTU Nicotinate-nucleotide pyrophosphorylase [carboxylating] (Gene Name=nadC)

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