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Crystal structure of the P450 BM3 heme domain mutant F87A/T268V/A82T/I263L in complex with N-imidazolyl-hexanoyl-L-phenylalanine, p-cresol and hydroxylamine

X-ray diffraction
1.99Å resolution
PDB entry 7y0p coloured by chain, front view.
PDB entry 7y0p coloured by chain, side view.
PDB entry 7y0p coloured by chain, top view.
Source organism: Priestia megaterium NBRC 15308 = ATCC 14581
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Bifunctional cytochrome P450/NADPH--P450 reductase
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Multimeric state: homo dimer
Accessible surface area: 32815.76 Å2
Buried surface area: 5201.73 Å2
Dissociation area: 703.34 Å2
Dissociation energy (ΔGdiss): -9.21 kcal/mol
Dissociation entropy (TΔSdiss): 13.91 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-147081

Macromolecules

Bifunctional cytochrome P450/NADPH--P450 reductase
Chains: A, B
Length: 465 amino acids
Theoretical weight: 53.38 KDa
Source organism: Priestia megaterium NBRC 15308 = ATCC 14581
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14779 (Residues: 1-456; Coverage: 44%)
Gene names: BG04_163, cyp102, cyp102A1
Pfam: Cytochrome P450
Bifunctional cytochrome P450/NADPH--P450 reductase in PDB entry 7y0p, assembly 1, front view.
Bifunctional cytochrome P450/NADPH--P450 reductase in PDB entry 7y0p, assembly 1, side view.
Bifunctional cytochrome P450/NADPH--P450 reductase in PDB entry 7y0p, assembly 1, top view.
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