7wg0

X-ray diffraction
2.2Å resolution

Structure of the Manganese Protoporphyrin IX-Reconstituted CYP102A1 Heme Domain with N-palmitoyl-L-phenylalanine

Released:
Model geometry
Fit model/data
Source organism: Priestia megaterium
Entry authors: Keita O, Osami S, Yuichiro A, Hiroshi S

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 483 amino acids
Theoretical weight: 55.1 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 1-457; Coverage: 44%)
Gene names: BG04_163, cyp102, cyp102A1
Sequence domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand MNH 2 x MNH
1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P212121
Unit cell:
a: 58.78Å b: 127.89Å c: 148.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.267
Expression system: Escherichia coli