› 4qck

X-ray diffraction
2.46Å resolution

Crystal structure of 3-ketosteroid-9-alpha-hydroxylase (KshA) from M. tuberculosis in complex with 4-androstene-3,17-dione

Released:
DOI: 10.2210/pdb4qck/pdb
PDB entry 4qck coloured by chain, front view.
PDB entry 4qck coloured by chain, side view.
PDB entry 4qck coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Substrate specificities and conformational flexibility of 3-ketosteroid 9α-hydroxylases.
Penfield JS, Worrall LJ, Strynadka NC, Eltis LD
J Biol Chem 289 25523-36 (2014)
PMID: 25049233

Function and Biology Details

Reaction catalysed: 
Androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 9-alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159823 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-ketosteroid-9-alpha-monooxygenase, oxygenase component Chain: A
Molecule details ›
Chain: A
Length: 386 amino acids
Theoretical weight: 44.33 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P71875 (Residues: 1-386; Coverage: 100%)
Gene names: Rv3526, kshA
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand FE 1 x FE
Ligand FES 1 x FES
Ligand PO4 1 x PO4
Ligand ASD 1 x ASD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P321
Unit cell:
a: 115.8Å b: 115.8Å c: 80.81Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.177 0.235
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.
Kal et al. (2017)
2 more

3 mentions without citation

Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.
Szaleniec et al. (2018)
2 more