3fwf

Ferric camphor bound cytochrome P450cam containing a Selenocysteine as the 5th heme ligand, monoclinic crystal form

Method: X-RAY DIFFRACTION Dmax: 111.2 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Camphor 5-monooxygenase

Pseudomonas putida

UniProt P00183

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 11–415 Mutation:C357U, R365L, E366Q HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CAM CAMPHOR × 1 K POTASSIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;277 K;24 % PEG 4000, 250 mM KCl, 50 mM TrisHCl, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.83 Å R-free 0.207
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 11–415 Mutation:C357U, R365L, E366Q HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CAM CAMPHOR × 1 K POTASSIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;277 K;24 % PEG 4000, 250 mM KCl, 50 mM TrisHCl, pH 7.4, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 1.83 Å R-free 0.207

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

128 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPXA_PSEPU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–405; UniProt 11–415 Author chain B; PDBConstruct 1–405; UniProt 11–415

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 3fwf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fwf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fwf
Deposition date deposition_date2009-01-18
Structure title titleFerric camphor bound cytochrome P450cam containing a Selenocysteine as the 5th heme ligand, monoclinic crystal form
Keywords keywordsSelenocysteine, Hemoprotein, Cytochrome P450, Cytochrome, Heme, Iron, Metal-binding, Monooxygenase, Oxidoreductase; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier33.97
Radius of gyration Rg (electron density) rg_electron33.54
Forward intensity I(0) i0131529000.00
Molecular weight molecular_weight92736.0 kDa
Excluded volume excluded_volume116220 ų
Envelope volume envelope_volume141490 ų
Hydration-shell volume shell_volume36435 ų
Envelope diameter envelope_diameter119.2
Shell Rg shell_rg38.70
Envelope Rg envelope_rg33.34
Shape Rg shape_rg33.57
Total Rg total_rg33.85
Total atoms total_atoms6514
Residues n_residues809
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax111.2
Rg (real space) rg_real34.14
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.3150e+08
I(0) uncertainty (real space) i0_real_error2.1470e+06
Rg (reciprocal space) rg_reciprocal34.04
I(0) (reciprocal space) i0_reciprocal131500000.0000
Solution quality estimate total_estimate0.8579
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.8
Skewness Skewness skewness0.433
Kurtosis Kurtosis kurtosis-0.535
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40320000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.827; Smooth: 0.825

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3fwfa_
Class classa — All alpha proteins
Fold Fold folda.104 — Cytochrome P450
Superfamily Superfamily superfamilya.104.1 — Cytochrome P450
Family Family familya.104.1.1 — Cytochrome P450
Domain ID domain_idd3fwfb_
Class classa — All alpha proteins
Fold Fold folda.104 — Cytochrome P450
Superfamily Superfamily superfamilya.104.1 — Cytochrome P450
Family Family familya.104.1.1 — Cytochrome P450

CATH v4.4 (2 domains)

Domain ID domain_id3fwfA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology630 — Cytochrome p450
Homologous superfamily homologous superfamily10 — Cytochrome P450
Domain ID domain_id3fwfB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology630 — Cytochrome p450
Homologous superfamily homologous superfamily10 — Cytochrome P450

8. Citations (1)

9. Files and Curves (10)