› 4yl2

X-ray diffraction
1.9Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175022 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-lactate oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 374 amino acids
Theoretical weight: 40.83 KDa
Source organism: Aerococcus viridans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q44467 (Residues: 1-374; Coverage: 100%)
Sequence domains: FMN-dependent dehydrogenase
Structure domains: Aldolase class I

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 134.852Å b: 119.081Å c: 106.81Å
α: 90° β: 121.3° γ: 90°
R-values:
R R work R free
0.185 0.183 0.228
Expression system: Escherichia coli BL21

Quick links

Citations

4 citation in other articles

Structure and role for active site lid of lactate monooxygenase from Mycobacterium smegmatis.
Kean et al. (2019)
3 more

2 mentions without citation

Conformational flexibility related to enzyme activity: evidence for a dynamic active-site gatekeeper function of Tyr(215) in Aerococcus viridans lactate oxidase.
Stoisser et al. (2016)
1 more