› 2jjn

X-ray diffraction
1.59Å resolution

Structure of closed cytochrome P450 EryK

Released:
DOI: 10.2210/pdb2jjn/pdb
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PDB entry 2jjn coloured by chain, front view.
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Source organism: Saccharopolyspora erythraea
Primary publication:
Investigating the structural plasticity of a cytochrome P450: three-dimensional structures of P450 EryK and binding to its physiological substrate.
Savino C, Montemiglio LC, Sciara G, Miele AE, Kendrew SG, Jemth P, Gianni S, Vallone B
J Biol Chem 284 29170-9 (2009)
PMID: 19625248

Function and Biology Details

Reaction catalysed: 
Erythromycin D + NADPH + O(2) = erythromycin C + NADP(+) + 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-155783 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Erythromycin C-12 hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 411 amino acids
Theoretical weight: 45.35 KDa
Source organism: Saccharopolyspora erythraea
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P48635 (Residues: 1-397; Coverage: 100%)
Gene names: CYP113A1, SACE_0713, eryK
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 53.46Å b: 68.004Å c: 57.407Å
α: 90° β: 101.05° γ: 90°
R-values:
R R work R free
0.162 0.16 0.195
Expression system: Escherichia coli BL21

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Citations

3 review citations

Diversity of P450 enzymes in the biosynthesis of natural products.
Podust et al. (2012)
2 more

4 mentions without citation

Metabolism of the Endocannabinoid Anandamide: Open Questions after 25 Years.
Maccarrone M. (2017)
3 more

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