› 3zkp

X-ray diffraction
2Å resolution

Structure of a mutant of P450 EryK in complex with erythromycin B.

Released:
DOI: 10.2210/pdb3zkp/pdb
PDB entry 3zkp coloured by chain, front view.
PDB entry 3zkp coloured by chain, side view.
PDB entry 3zkp coloured by chain, top view.
Source organism: Saccharopolyspora erythraea NRRL 2338
Primary publication:
Redirecting P450 EryK specificity by rational site-directed mutagenesis.
Montemiglio LC, Macone A, Ardiccioni C, Avella G, Vallone B, Savino C
Biochemistry 52 3678-87 (2013)
PMID: 23597312

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: 45.29 KDa
Source organism: Saccharopolyspora erythraea NRRL 2338
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 ERB 1 x ERB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 57.753Å b: 36.597Å c: 96.273Å
α: 90° β: 92.93° γ: 90°
R-values:
R R work R free
0.166 0.163 0.215
Expression system: Escherichia coli BL21

Quick links

Citations

3 citation in other articles

Engineering of global regulator cAMP receptor protein (CRP) in Escherichia coli for improved lycopene production.
Huang et al. (2015)
2 more