› 3h5e

X-ray diffraction
2Å resolution

LeuD_1-156 small subunit of isopropylmalate isomerase (Rv2987c) from mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb3h5e/pdb
PDB entry 3h5e coloured by chain, front view.
PDB entry 3h5e coloured by chain, side view.
PDB entry 3h5e coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural studies on the enzyme complex isopropylmalate isomerase (LeuCD) from Mycobacterium tuberculosis.
Manikandan K, Geerlof A, Zozulya AV, Svergun DI, Weiss MS
Proteins 79 35-49 (2011)
PMID: 20938981

Function and Biology Details

Reaction catalysed: 
(1a) (2R,3S)-3-isopropylmalate = 2-isopropylmaleate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161730 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-isopropylmalate dehydratase small subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.25 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WK95 (Residues: 2-156; Coverage: 78%)
Gene names: MTV012.01c, Rv2987c, leuD
Sequence domains: Aconitase C-terminal domain
Structure domains: Aconitase, domain 4

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6522
Unit cell:
a: 64.62Å b: 64.62Å c: 419.82Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.234 0.269
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.
Yan et al. (2022)
10 other articles

2 mentions without citation

Bacterial Branched-Chain Amino Acid Biosynthesis: Structures, Mechanisms, and Drugability.
Amorim Franco et al. (2017)
1 more