› 5g2g

X-ray diffraction
1.6Å resolution

Crystal structure of ketosteroid isomerase containing M116K mutation in the equilenin-bound form

Released:
DOI: 10.2210/pdb5g2g/pdb
PDB entry 5g2g coloured by chain, front view.
PDB entry 5g2g coloured by chain, side view.
PDB entry 5g2g coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Role of conserved Met112 residue in the catalytic activity and stability of ketosteroid isomerase.
Cha HJ, Jang do S, Jeong JH, Hong BH, Yun YS, Shin EJ, Choi KY
Biochim Biophys Acta 1864 1322-7 (2016)
PMID: 27375051

Function and Biology Details

Reaction catalysed: 
A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)-steroid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139594 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Steroid Delta-isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 127 amino acids
Theoretical weight: 14.06 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P07445 (Residues: 2-128; Coverage: 97%)
Gene name: ksi
Sequence domains: SnoaL-like domain
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

1 bound ligand:
Ligand EQU 2 x EQU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P212121
Unit cell:
a: 35.525Å b: 73.582Å c: 95.214Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.23
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Accurate positioning of functional residues with robotics-inspired computational protein design.
Krivacic et al. (2022)