2l8m

Reduced and CO-bound cytochrome P450cam (CYP101A1)

Method: SOLUTION NMR Dmax: 71.8 Å Quality: REASONABLE

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 1–415 Fragment:sequence database residues 11-415 CAM CAMPHOR × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CMO CARBON MONOXIDE × 1 K POTASSIUM ION × 4 CL CHLORIDE ION × 3 SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:0.4 mM [U-100% 13C; U-100% 15N; U-80% 2H] reduced-CO-bound CYP101A1, 3 mM camphor, pH 7.4 TrisHCl buffer, 100 mM KCl cytochrome, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.4 mM [U-15N] reduced-CO-bound CYP101A1, 3 mM camphor, pH 7.4 TrisHCl buffer, 100 mM KCl, 5% nematic phase C12E5/hexanol added for alignment, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.4 mM [U-15N] reduced-CO-bound CYP101A1, 3 mM camphor, pH 7.4 TrisHCl buffer, 100 mM KCl, except 8 mg/mL pf1 phage added, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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 172 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 1–415; UniProt 1–415

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 2l8m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2l8m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2l8m
Deposition date deposition_date2011-01-19
Structure title titleReduced and CO-bound cytochrome P450cam (CYP101A1)
Keywords keywordsmetalloenzyme, monooxygenase, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier22.79
Radius of gyration Rg (electron density) rg_electron21.44
Forward intensity I(0) i036142600.00
Molecular weight molecular_weight46636.0 kDa
Excluded volume excluded_volume58443 ų
Envelope volume envelope_volume68364 ų
Hydration-shell volume shell_volume25947 ų
Envelope diameter envelope_diameter75.0
Shell Rg shell_rg28.97
Envelope Rg envelope_rg21.85
Shape Rg shape_rg21.41
Total Rg total_rg22.46
Total atoms total_atoms6474
Residues n_residues405
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 dmax71.8
Rg (real space) rg_real22.68
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real3.6140e+07
I(0) uncertainty (real space) i0_real_error4.4550e+05
Rg (reciprocal space) rg_reciprocal22.71
I(0) (reciprocal space) i0_reciprocal36140000.0000
Solution quality estimate total_estimate0.6990
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8500000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 0.130; Positv: 1.000; Valcen: 0.992; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2l8ma_
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 (1 domains)

Domain ID domain_id2l8mA00
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)