Structure of PDB 1qpr Chain C

Receptor sequence

>1qprC (length=284) Species: 83332 (Mycobacterium tuberculosis H37Rv)

GLSDWELAAARAAIARGLDEDLRYGPDVTTLATVPASATTTASLVTREAG
VVAGLDVALLTLNEVLGTNGYRVLDRVEDGARVPPGEALMTLEAQTRGLL
TAERTMLNLVGHLSGIATATAAWVDAVRGTKAKIRDTRKTLPGLRALQKY
AVRTGGGVNHRLGLGDAALIKDNHVAAAGSVVDALRAVRNAAPDLPCEVE
VDSLEQLDAVLPEKPELILLDNFAVWQTQTAVQRRDSRAPTVMLESSGGL
SLQTAATYAETGVDYLAVGALTHSVRVLDIGLDM

3D structure

• PDB: 1qpr Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target.
• Chain: C
• Resolution: 2.45 Å

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	C	E201 D222	E200 D221
BS02	PHT	C	T138 R139 H161 R162 L170 K172	T137 R138 H160 R161 L169 K171
BS03	PPC	C	K140 D222 S248 G270	K139 D221 S247 G269

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

External links

• PDB: RCSB:1qpr, PDBe:1qpr, PDBj:1qpr
• PDBsum: 1qpr
• PubMed: 9862811
• UniProt: P9WJJ7|NADC_MYCTU Nicotinate-nucleotide pyrophosphorylase [carboxylating] (Gene Name=nadC)