› 3s2y

X-ray diffraction
2.24Å resolution

Crystal structure of a chromate/uranium reductase from Gluconacetobacter hansenii

Released:
DOI: 10.2210/pdb3s2y/pdb
PDB entry 3s2y coloured by chain, front view.
PDB entry 3s2y coloured by chain, side view.
PDB entry 3s2y coloured by chain, top view.
Source organism: Komagataeibacter hansenii ATCC 23769
Primary publication:
Structure determination and functional analysis of a chromate reductase from Gluconacetobacter hansenii.
Jin H, Zhang Y, Buchko GW, Varnum SM, Robinson H, Squier TC, Long PE
PLoS One 7 e42432 (2012)
PMID: 22879982

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADPH-dependent FMN reductase-like domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 199 amino acids
Theoretical weight: 21.34 KDa
Source organism: Komagataeibacter hansenii ATCC 23769
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: D5QFC5 (Residues: 1-193; Coverage: 100%)
Gene name: GXY_09224
Sequence domains: NADPH-dependent FMN reductase
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand FMN 4 x FMN
Ligand CL 3 x CL
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 119.677Å b: 90.051Å c: 95.234Å
α: 90° β: 119.61° γ: 90°
R-values:
R R work R free
0.196 0.193 0.238
Expression system: Escherichia coli BL21

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Citations

2 review citations

Bacterial chromate reductase, a potential enzyme for bioremediation of hexavalent chromium: a review.
Thatoi et al. (2014)
1 more

3 mentions without citation

The structural and functional basis of catalysis mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans.
Sedláček et al. (2014)
2 more