› 2vcf

X-ray diffraction
1.8Å resolution

Structure of isoniazid (INH) bound to cytosolic soybean ascorbate peroxidase

Released:
DOI: 10.2210/pdb2vcf/pdb
PDB entry 2vcf coloured by chain, front view.
PDB entry 2vcf coloured by chain, side view.
PDB entry 2vcf coloured by chain, top view.
Source organism: Glycine max
Primary publication:
The tuberculosis prodrug isoniazid bound to activating peroxidases.
Metcalfe C, Macdonald IK, Murphy EJ, Brown KA, Raven EL, Moody PC
J Biol Chem 283 6193-200 (2008)
PMID: 18056997

Function and Biology Details

Reaction catalysed: 
(1a) 2 L-ascorbate + H(2)O(2) + 2 H(+) = 2 monodehydroascorbate + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174997 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ascorbate peroxidase Chain: X
Molecule details ›
Chain: X
Length: 264 amino acids
Theoretical weight: 28.76 KDa
Source organism: Glycine max
Expression system: Escherichia coli
UniProt:
  • Canonical: Q43758 (Residues: 2-250; Coverage: 100%)
Gene name: apx1
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
2 bound ligands:
Ligand ISZ 2 x ISZ
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P42212
Unit cell:
a: 82.243Å b: 82.243Å c: 74.965Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.154 0.188
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Overview on mechanisms of isoniazid action and resistance in Mycobacterium tuberculosis.
Unissa et al. (2016)
3 more

5 mentions without citation

Post-Translational Modification of Proteins Mediated by Nitro-Fatty Acids in Plants: Nitroalkylation.
Aranda-Caño et al. (2019)
4 more