› 5ket

X-ray diffraction
2.85Å resolution

Structure of the aldo-keto reductase from Coptotermes gestroi

Released:
DOI: 10.2210/pdb5ket/pdb
PDB entry 5ket coloured by chain, front view.
PDB entry 5ket coloured by chain, side view.
PDB entry 5ket coloured by chain, top view.
Source organism: Coptotermes gestroi
Primary publication:
The Coptotermes gestroi aldo-keto reductase: a multipurpose enzyme for biorefinery applications.
Tramontina R, Franco Cairo JP, Liberato MV, Mandelli F, Sousa A, Santos S, Rabelo SC, Campos B, Ienczak J, Ruller R, Damásio AR, Squina FM
Biotechnol Biofuels 10 4 (2017)
PMID: 28053664

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102918 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADP-dependent oxidoreductase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 340 amino acids
Theoretical weight: 38.35 KDa
Source organism: Coptotermes gestroi
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A140CVV2 (Residues: 1-334; Coverage: 100%)
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: R32
Unit cell:
a: 131.141Å b: 131.141Å c: 290.657Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.242 0.239 0.293
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.
Bissaro et al. (2018)
6 other articles

1 mention without citation

The Coptotermes gestroi aldo-keto reductase: a multipurpose enzyme for biorefinery applications.
Tramontina et al. (2017)