Structure of PDB 1qpn Chain F

Receptor sequence
>1qpnF (length=284) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
GLSDWELAAARAAIARGLDEDLRYGPDVTTLATVPASATTTASLVTREAG
VVAGLDVALLTLNEVLGTNGYRVLDRVEDGARVPPGEALMTLEAQTRGLL
TAERTMLNLVGHLSGIATATAAWVDAVRGTKAKIRDTRKTLPGLRALQKY
AVRTGGGVNHRLGLGDAALIKDNHVAAAGSVVDALRAVRNAAPDLPCEVE
VDSLEQLDAVLPEKPELILLDNFAVWQTQTAVQRRDSRAPTVMLESSGGL
SLQTAATYAETGVDYLAVGALTHSVRVLDIGLDM
3D structure
PDB1qpn Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target.
ChainF
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R2605 K2640 K2672 E2701 D2722
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 NCN F T2638 K2640 H2661 R2662 S2748 G2749 A2768 G2770 H2774 T137 K139 H160 R161 S247 G248 A267 G269 H273
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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Biological Process
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Cellular Component
External links
PDB RCSB:1qpn, PDBe:1qpn, PDBj:1qpn
PDBsum1qpn
PubMed9862811
UniProtP9WJJ7|NADC_MYCTU Nicotinate-nucleotide pyrophosphorylase [carboxylating] (Gene Name=nadC)

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