› 1qpn

X-ray diffraction
2.6Å resolution

Quinolinate Phosphoribosyl Transferase from Mycobacterium Tuberculosis in Complex with NCNN

Released:
DOI: 10.2210/pdb1qpn/pdb
PDB entry 1qpn coloured by chain, front view.
PDB entry 1qpn coloured by chain, side view.
PDB entry 1qpn coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Crystal structure of quinolinic acid phosphoribosyltransferase from Mmycobacterium tuberculosis: a potential TB drug target.
Sharma V, Grubmeyer C, Sacchettini JC
Structure 6 1587-99 (1998)
PMID: 9862811

Function and Biology Details

Reaction catalysed: 
Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161695 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinate-nucleotide pyrophosphorylase [carboxylating] Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 284 amino acids
Theoretical weight: 29.85 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WJJ7 (Residues: 2-285; Coverage: 100%)
Gene names: MTCY336.08c, Rv1596, nadC
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NCN 6 x NCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P31
Unit cell:
a: 100.383Å b: 100.383Å c: 144.61Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 0.269
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions.
Nagano et al. (2002)
10 more

5 mentions without citation

Comparative biochemical and computational study of the role of naturally occurring mutations at Ambler positions 104 and 170 in GES β-lactamases.
Kotsakis et al. (2010)
4 more