› 3krz

X-ray diffraction
1.8Å resolution

Crystal Structure of the Thermostable NADH4-bound old yellow enzyme from Thermoanaerobacter pseudethanolicus E39

Released:
DOI: 10.2210/pdb3krz/pdb
PDB entry 3krz coloured by chain, front view.
PDB entry 3krz coloured by chain, side view.
PDB entry 3krz coloured by chain, top view.
Source organism: Thermoanaerobacter pseudethanolicus ATCC 33223
Primary publication:
Biocatalysis with thermostable enzymes: structure and properties of a thermophilic 'ene'-reductase related to old yellow enzyme.
Adalbjörnsson BV, Toogood HS, Fryszkowska A, Pudney CR, Jowitt TA, Leys D, Scrutton NS
Chembiochem 11 197-207 (2010)
PMID: 19943268

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109165 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH:flavin oxidoreductase/NADH oxidase N-terminal domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 337 amino acids
Theoretical weight: 38.23 KDa
Source organism: Thermoanaerobacter pseudethanolicus ATCC 33223
Expression system: Escherichia coli
UniProt:
  • Canonical: B0KAH1 (Residues: 1-337; Coverage: 100%)
Gene name: Teth39_0012
Sequence domains: NADH:flavin oxidoreductase / NADH oxidase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand FMN 4 x FMN
Ligand TXD 4 x TXD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 87.38Å b: 98.556Å c: 95.134Å
α: 90° β: 92.4° γ: 90°
R-values:
R R work R free
0.157 0.157 0.194
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Stabilizing biocatalysts.
Bommarius et al. (2013)
2 more

1 mention without citation

Catalytic Performance of a Class III Old Yellow Enzyme and Its Cysteine Variants.
Scholtissek et al. (2018)