› 2bcp

X-ray diffraction
2.1Å resolution

Structural Analysis of Streptococcus pyogenes NADH oxidase: C44S Nox with Azide

Released:
DOI: 10.2210/pdb2bcp/pdb
PDB entry 2bcp coloured by chain, front view.
PDB entry 2bcp coloured by chain, side view.
PDB entry 2bcp coloured by chain, top view.
Source organism: Streptococcus pyogenes
Primary publication:
Structural Analysis of Streptococcus pyogenes NADH Oxidase: Conformational Dynamics Involved in Formation of the C(4a)-Peroxyflavin Intermediate.
Wallen JR, Mallett TC, Okuno T, Parsonage D, Sakai H, Tsukihara T, Claiborne A
Biochemistry 54 6815-29 (2015)
PMID: 26506002

Function and Biology Details

Reaction catalysed: 
2 NADH + O(2) = 2 NAD(+) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 490 amino acids
Theoretical weight: 53.44 KDa
Source organism: Streptococcus pyogenes
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5XC60 (Residues: 2-456; Coverage: 100%)
Gene name: M6_Spy0868
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand AZI 2 x AZI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P212121
Unit cell:
a: 71.32Å b: 85.085Å c: 148.456Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.236
Expression system: Escherichia coli

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Citations

1 review citation

Lone pair-π interactions in biological systems: occurrence, function, and physical origin.
Kozelka J. (2017)
5 other articles