› 3aty

X-ray diffraction
1.7Å resolution

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-184702 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH:flavin oxidoreductase/NADH oxidase N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 379 amino acids
Theoretical weight: 42.31 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8I6L9 (Residues: 1-379; Coverage: 100%)
Gene names: ECC02_012910, ECC02_013670, TcPGFS
Sequence domains: NADH:flavin oxidoreductase / NADH oxidase family
Structure domains: Aldolase class I

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 56.291Å b: 78.791Å c: 78.797Å
α: 90° β: 93.37° γ: 90°
R-values:
R R work R free
0.17 0.17 0.195
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Old yellow enzymes: structures and structure-guided engineering for stereocomplementary bioreduction.
Shi et al. (2020)
3 other articles

5 mentions without citation

Enzymes of the cyclooxygenase pathways of prostanoid biosynthesis.
Smith et al. (2011)
4 more