› 3ks0

X-ray diffraction
2.7Å resolution

Crystal structure of the heme domain of flavocytochrome b2 in complex with Fab B2B4

Released:
DOI: 10.2210/pdb3ks0/pdb
PDB entry 3ks0 coloured by chain, front view.
PDB entry 3ks0 coloured by chain, side view.
PDB entry 3ks0 coloured by chain, top view.
Source organisms:
Primary publication:
Structural evidence for the functional importance of the heme domain mobility in flavocytochrome b2.
Diêp Lê KH, Lederer F, Golinelli-Pimpaneau B
J Mol Biol 400 518-30 (2010)
PMID: 20546754

Function and Biology Details

Reaction catalysed: 
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-208201 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
heme domain of flavocytochrome b2 Chains: J, L
Molecule details ›
Chains: J, L
Length: 214 amino acids
Theoretical weight: 22.88 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Fragment Antigen Binding B2B4 Chains: H, K
Molecule details ›
Chains: H, K
Length: 225 amino acids
Theoretical weight: 24.48 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
L-lactate dehydrogenase (cytochrome) Chains: A, B
Molecule details ›
Chains: A, B
Length: 95 amino acids
Theoretical weight: 10.46 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P00175 (Residues: 86-180; Coverage: 16%)
Gene names: CYB2, YM9958.08C, YML054C
Sequence domains: Cytochrome b5-like Heme/Steroid binding domain
Structure domains: Cytochrome b5-like heme/steroid binding domain

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 72.58Å b: 83.68Å c: 92.165Å
α: 90° β: 96.8° γ: 90°
R-values:
R R work R free
0.218 0.214 0.289
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Microbial lactate utilization: enzymes, pathogenesis, and regulation.
Jiang et al. (2014)
2 more

5 mentions without citation

Toward a hepatitis C virus vaccine: the structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody.
Potter et al. (2012)
4 more