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1cpt

CRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 68.1 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CYTOCHROME P450-TERP

Pseudomonas sp.

UniProt P33006

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 1–428 Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.30 Å

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.

Other PDB Difference from Current Entry 1CPT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8EUH cytochrome P450terp (cyp108A1) bound to alpha-terpineol Deposited 2022-10-18 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–428（428 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 XGE alpha-TERPINEOL × 2 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.06 M magnesium chloride hexahyrate, 0.06 M calcium chloride dihydrate, 0.1 M sodium HEPES and MOPS (acid) pH 7.5, 20% v/v ethylene glycol, 10% v/v PEG 8000
Resolution 2.00 Å R-free 0.210
8EUK cytochrome P450terp (cyp108A1) bound to ethylene glycol Deposited 2022-10-18 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–428（428 aa）
Not recorded HEM PROTOPORPHYRIN IX CONTAINING FE × 1 EDO 1,2-ETHANEDIOL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.06 M magnesium chloride hexahyrate, 0.06 M calcium chloride dihydrate, 0.1 M sodium HEPES and MOPS (acid) pH 7.5, 20% v/v ethylene glycol, 10% v/v PEG 8000
Resolution 1.98 Å R-free 0.206
8EUL cytochrome P450terp (cyp108A1) mutant F188A bound to alpha-terpineol Deposited 2022-10-18 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–428（428 aa）
Mutation：F188A HEM PROTOPORPHYRIN IX CONTAINING FE × 1 XGE alpha-TERPINEOL × 1 EDO 1,2-ETHANEDIOL × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.06 M magnesium chloride hexahyrate, 0.06 M calcium chloride dihydrate, 0.1 M sodium HEPES and MOPS (acid) pH 7.5, 20% v/v ethylene glycol, 10% v/v PEG 8000, saturating alpha-terpineol
Resolution 2.24 Å R-free 0.224

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPXL_PSESP
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–428； UniProt 1–428

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 1cpt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cpt
Deposition date deposition_date1993-11-23
Structure title titleCRYSTAL STRUCTURE AND REFINEMENT OF CYTOCHROME P450-TERP AT 2.3 ANGSTROMS RESOLUTION
Keywords keywordsOXIDOREDUCTASE(OXYGENASE); OXIDOREDUCTASE(OXYGENASE)
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.53 Å
Radius of gyration Rg (electron density) rg_electron21.31 Å
Forward intensity I(0) i036574500.00
Molecular weight molecular_weight46765.0 kDa
Excluded volume excluded_volume58455 ų
Envelope volume envelope_volume67226 ų
Hydration-shell volume shell_volume25773 ų
Envelope diameter envelope_diameter70.1 Å
Shell Rg shell_rg28.57 Å
Envelope Rg envelope_rg21.45 Å
Shape Rg shape_rg21.29 Å
Total Rg total_rg22.20 Å
Total atoms total_atoms3292
Residues n_residues412
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax68.1 Å
Rg (real space) rg_real22.40 Å
Rg uncertainty (real space) rg_real_error0.28 Å
I(0) (real space) i0_real3.6570e+07
I(0) uncertainty (real space) i0_real_error4.7010e+05
Rg (reciprocal space) rg_reciprocal22.44 Å
I(0) (reciprocal space) i0_reciprocal36580000.0000
Solution quality estimate total_estimate0.9079
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9 Å
Skewness Skewness skewness0.139
Kurtosis Kurtosis kurtosis-0.543
Angular range angular_range— – 0.3550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7717000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.971
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cpta_
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_id1cptA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology630 — Cytochrome p450
Homologous superfamily homologous superfamily10 — Cytochrome P450
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8. Citations (3)

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9. Files and Curves (10)