1k2o

Cytochrome P450Cam with Bound BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II)

Method: X-RAY DIFFRACTION Dmax: 93.4 Å Quality: EXCELLENT

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

Cytochrome P450CAM

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 1–414 Mutation:C334A CAC CACODYLATE ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 RFA DELTA-BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II) × 1 RFB LAMBDA-BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:SLOW COOLING;pH 7.5;277 K;Hepes, PEG, KCL, DTT, pH 7.5, slow cooling, temperature 277K Resolution 1.65 Å R-free 0.226
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–414 Mutation:C334A CAC CACODYLATE ION × 3 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 RFA DELTA-BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II) × 1 RFB LAMBDA-BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:SLOW COOLING;pH 7.5;277 K;Hepes, PEG, KCL, DTT, pH 7.5, slow cooling, temperature 277K Resolution 1.65 Å R-free 0.226

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 1–414; UniProt 1–414 Author chain B; PDBConstruct 1–414; UniProt 1–414

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 1k2o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k2o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k2o
Deposition date deposition_date2001-09-28
Structure title titleCytochrome P450Cam with Bound BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II)
Keywords keywords;P450, monooxygenase, electron transfer, energy transfer, fluorinated aromatics, biphenyl, adamantane, ruthenium channel, substrate-binding, OXIDOREDUCTASE ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.13
Radius of gyration Rg (electron density) rg_electron29.09
Forward intensity I(0) i0143957000.00
Molecular weight molecular_weight95219.0 kDa
Excluded volume excluded_volume119000 ų
Envelope volume envelope_volume141710 ų
Hydration-shell volume shell_volume39711 ų
Envelope diameter envelope_diameter98.7
Shell Rg shell_rg37.15
Envelope Rg envelope_rg29.00
Shape Rg shape_rg29.10
Total Rg total_rg29.75
Total atoms total_atoms6670
Residues n_residues812
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 dmax93.4
Rg (real space) rg_real30.02
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real1.4400e+08
I(0) uncertainty (real space) i0_real_error2.1730e+06
Rg (reciprocal space) rg_reciprocal30.07
I(0) (reciprocal space) i0_reciprocal144000000.0000
Solution quality estimate total_estimate0.9075
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.205
Kurtosis Kurtosis kurtosis-0.536
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40040000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1k2oa_
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_idd1k2ob_
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_id1k2oA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology630 — Cytochrome p450
Homologous superfamily homologous superfamily10 — Cytochrome P450
Domain ID domain_id1k2oB00
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)