› 2bpq

X-ray diffraction
1.9Å resolution

Anthranilate phosphoribosyltransferase (TrpD) from Mycobacterium tuberculosis (Apo structure)

Released:
DOI: 10.2210/pdb2bpq/pdb
PDB entry 2bpq coloured by chain, front view.
PDB entry 2bpq coloured by chain, side view.
PDB entry 2bpq coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
The crystal structure of TrpD, a metabolic enzyme essential for lung colonization by Mycobacterium tuberculosis, in complex with its substrate phosphoribosylpyrophosphate.
Lee CE, Goodfellow C, Javid-Majd F, Baker EN, Shaun Lott J
J Mol Biol 355 784-97 (2006)
PMID: 16337227

Function and Biology Details

Reaction catalysed: 
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161439 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Anthranilate phosphoribosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 373 amino acids
Theoretical weight: 38 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WFX5 (Residues: 1-370; Coverage: 100%)
Gene names: MTCY190.03c, Rv2192c, trpD
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand BEN 3 x BEN
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P212121
Unit cell:
a: 80.874Å b: 82.415Å c: 117.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Structural genomics approach to drug discovery for Mycobacterium tuberculosis.
Ioerger et al. (2009)
6 more

5 mentions without citation

The tryptophan biosynthetic pathway is essential for Mycobacterium tuberculosis to cause disease.
Lott JS. (2020)
4 more