X-ray diffraction
1.9Å resolution

Crystal structure of aldo-keto reductase from Polaromonas sp. JS666

Source organism: Polaromonas sp. JS666
Entry authors: Gasiorowska OA, Handing KB, Shabalin IG, Sroka P, Hillerich BS, Bonanno J, Seidel R, Almo SC, Minor W, New York Structural Genomics Research Consortium (NYSGRC)

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Aldo_ket_red domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 344 amino acids
Theoretical weight: 37.41 KDa
Source organism: Polaromonas sp. JS666
Expression system: Escherichia coli
  • Canonical: Q124A1 (Residues: 1-343; Coverage: 100%)
Gene name: Bpro_4249
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I422
Unit cell:
a: 105.11Å b: 105.11Å c: 479.569Å
α: 90° β: 90° γ: 90°
R R work R free
0.162 0.16 0.185
Expression system: Escherichia coli