› 5l91

X-ray diffraction
2.2Å resolution

The 2.2 A crystal structure of CYP109E1 from Bacillus megaterium bound with four corticosterone molecules

Released:
DOI: 10.2210/pdb5l91/pdb
PDB entry 5l91 coloured by chain, front view.
PDB entry 5l91 coloured by chain, side view.
PDB entry 5l91 coloured by chain, top view.
Source organism: Priestia megaterium DSM 319
Primary publication:
Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium.
Jóźwik IK, Kiss FM, Gricman Ł, Abdulmughni A, Brill E, Zapp J, Pleiss J, Bernhardt R, Thunnissen AW
FEBS J 283 4128-4148 (2016)
PMID: 27686671

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-112687 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 Chains: A, B
Molecule details ›
Chains: A, B
Length: 410 amino acids
Theoretical weight: 47.82 KDa
Source organism: Priestia megaterium DSM 319
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D5DKI8 (Residues: 1-404; Coverage: 100%)
Gene name: BMD_3874
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

2 bound ligands:
Ligand HEM 2 x HEM
Ligand C0R 8 x C0R
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P3221
Unit cell:
a: 120.418Å b: 120.418Å c: 140.803Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.185 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Bacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.
Szaleniec et al. (2018)
3 more

2 mentions without citation

Structural basis of steroid binding and oxidation by the cytochrome P450 CYP109E1 from Bacillus megaterium.
Jóźwik et al. (2016)
1 more