4ast

X-ray diffraction
2.38Å resolution

The apo structure of a bacterial aldo-keto reductase AKR14A1

Released:
Source organism: Escherichia coli K-12
Primary publication:
The diversity of microbial aldo/keto reductases from Escherichia coli K12.
Chem Biol Interact 202 168-77 (2013)
PMID: 23103600

Function and Biology Details

Structure analysis Details

Assembly composition:
homo octamer (preferred)
PDBe Complex ID:
PDB-CPX-175143 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-glyceraldehyde 3-phosphate reductase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 346 amino acids
Theoretical weight: 38.88 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q46851 (Residues: 1-346; Coverage: 100%)
Gene names: JW2970, b3001, gpr, mgrA, yghZ
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 98.808Å b: 144.317Å c: 113.896Å
α: 90° β: 96.51° γ: 90°
R-values:
R R work R free
0.241 0.239 0.279
Expression system: Escherichia coli BL21(DE3)