› 2whw

X-ray diffraction
2.2Å resolution

Selective oxidation of carbolide C-H bonds by engineered macrolide P450 monooxygenase

Released:
DOI: 10.2210/pdb2whw/pdb
PDB entry 2whw coloured by chain, front view.
PDB entry 2whw coloured by chain, side view.
PDB entry 2whw coloured by chain, top view.
Source organism: Streptomyces venezuelae
Primary publication:
Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase.
Li S, Chaulagain MR, Knauff AR, Podust LM, Montgomery J, Sherman DH
Proc Natl Acad Sci U S A 106 18463-8 (2009)
PMID: 19833867

Function and Biology Details

Reaction catalysed: 
10-deoxymethymycin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = methymycin + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131501 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 monooxygenase PikC Chains: A, B
Molecule details ›
Chains: A, B
Length: 436 amino acids
Theoretical weight: 48.18 KDa
Source organism: Streptomyces venezuelae
Expression system: Escherichia coli
UniProt:
  • Canonical: O87605 (Residues: 1-416; Coverage: 100%)
Gene names: picK, pikC
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

3 bound ligands:
Ligand HEM 2 x HEM
Ligand 1D4 2 x 1D4
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 60.182Å b: 109.536Å c: 153.261Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.177 0.256
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Mechanical properties of cellularly responsive hydrogels and their experimental determination.
Kloxin et al. (2010)
13 more

4 mentions without citation

Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.
Rudolf et al. (2017)
3 more