› 4hgg

X-ray diffraction
1.7Å resolution

Crystal structure of P450 BM3 5F5R heme domain variant complexed with styrene

Released:
DOI: 10.2210/pdb4hgg/pdb
PDB entry 4hgg coloured by chain, front view.
PDB entry 4hgg coloured by chain, side view.
PDB entry 4hgg coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation.
Shehzad A, Panneerselvam S, Linow M, Bocola M, Roccatano D, Mueller-Dieckmann J, Wilmanns M, Schwaneberg U
Chem Commun (Camb) 49 4694-6 (2013)
PMID: 23589805

Function and Biology Details

Reactions catalysed: 
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional cytochrome P450/NADPH--P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 52.15 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14779 (Residues: 2-456; Coverage: 43%)
Gene names: BG04_163, cyp102, cyp102A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
3 bound ligands:
Ligand SYN 2 x SYN
Ligand MES 1 x MES
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21
Unit cell:
a: 58.9Å b: 147.98Å c: 64.01Å
α: 90° β: 98.37° γ: 90°
R-values:
R R work R free
0.18 0.179 0.211
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Improving and repurposing biocatalysts via directed evolution.
Denard et al. (2015)
5 other articles