› 4m5p

X-ray diffraction
1.5Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107165 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH:flavin oxidoreductase/NADH oxidase N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 407 amino acids
Theoretical weight: 45.34 KDa
Source organism: Scheffersomyces stipitis CBS 6054
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A3LT82 (Residues: 1-407; Coverage: 100%)
Gene names: OYE2.6, PICST_44614
Sequence domains: NADH:flavin oxidoreductase / NADH oxidase family
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand FMN 1 x FMN
Ligand MLA 3 x MLA
Ligand NA 3 x NA
Ligand 23W 1 x 23W
1 modified residue:
Ligand CSD 1 x CSD

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P6322
Unit cell:
a: 126.487Å b: 126.487Å c: 123.307Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.144 0.141 0.17
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Biocatalytic Reduction Reactions from a Chemist's Perspective.
Hollmann et al. (2021)
3 more

1 mention without citation

Residues Controlling Facial Selectivity in an Alkene Reductase and Semirational Alterations to Create Stereocomplementary Variants.
Walton et al. (2014)