› 2dhq

X-ray diffraction
2Å resolution

3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS

Released:
DOI: 10.2210/pdb2dhq/pdb
PDB entry 2dhq coloured by chain, front view.
PDB entry 2dhq coloured by chain, side view.
PDB entry 2dhq coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.
Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L
Nat Struct Biol 6 521-5 (1999)
PMID: 10360352

Function and Biology Details

Reaction catalysed: 
3-dehydroquinate = 3-dehydroshikimate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo decamer (preferred)
homo dodecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-162015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-dehydroquinate dehydratase Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 15.68 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPX7 (Residues: 2-147; Coverage: 99%)
Gene names: MTCY159.19, Rv2537c, aroD, aroQ
Sequence domains: Dehydroquinase class II
Structure domains: Dehydroquinase, class II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: F23
Unit cell:
a: 127.68Å b: 127.68Å c: 127.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.147 0.196
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Structural biology and drug discovery of difficult targets: the limits of ligandability.
Surade et al. (2012)
8 more

6 mentions without citation

3D complex: a structural classification of protein complexes.
Levy et al. (2006)
5 more