4jb4

Expression, Purification, Characterization, and Solution NMR Study of Highly Deuterated Yeast Cytochrome c Peroxidase with Enhanced Solubility

Method: X-RAY DIFFRACTION Dmax: 92.9 Å Quality: GOOD

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

Cytochrome c peroxidase, mitochondrial

Saccharomyces cerevisiae

UniProt P00431

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 68–361 Fragment:cytochrome-c peroxidase, UNP residues 68-361 Mutation:T1M, T2K, P3T HEM PROTOPORPHYRIN IX CONTAINING FE × 1 F FLUORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;0.2M NH4Cl, 0.1 M CH3COONa pH5.0 and 20% w/v PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.39 Å R-free 0.279
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 68–361 Fragment:cytochrome-c peroxidase, UNP residues 68-361 Mutation:T1M, T2K, P3T HEM PROTOPORPHYRIN IX CONTAINING FE × 1 F FLUORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;0.2M NH4Cl, 0.1 M CH3COONa pH5.0 and 20% w/v PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.39 Å R-free 0.279

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.

175 other PDB entries and 192 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CCPR_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–294; UniProt 68–361 Author chain C; PDBConstruct 1–294; UniProt 68–361

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 4jb4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4jb4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4jb4
Deposition date deposition_date2013-02-19
Structure title titleExpression, Purification, Characterization, and Solution NMR Study of Highly Deuterated Yeast Cytochrome c Peroxidase with Enhanced Solubility
Keywords keywordsCytochrome c Peroxidase, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.62
Radius of gyration Rg (electron density) rg_electron28.25
Forward intensity I(0) i073603800.00
Molecular weight molecular_weight67679.0 kDa
Excluded volume excluded_volume84450 ų
Envelope volume envelope_volume101650 ų
Hydration-shell volume shell_volume30279 ų
Envelope diameter envelope_diameter97.1
Shell Rg shell_rg35.06
Envelope Rg envelope_rg28.40
Shape Rg shape_rg28.23
Total Rg total_rg28.94
Total atoms total_atoms4792
Residues n_residues582
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 dmax92.9
Rg (real space) rg_real28.71
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real7.3600e+07
I(0) uncertainty (real space) i0_real_error1.1750e+06
Rg (reciprocal space) rg_reciprocal28.67
I(0) (reciprocal space) i0_reciprocal73600000.0000
Solution quality estimate total_estimate0.8762
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.409
Kurtosis Kurtosis kurtosis-0.466
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15880000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.916; Smooth: 0.869

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4jb4a_
Class classa — All alpha proteins
Fold Fold folda.93 — Heme-dependent peroxidases
Superfamily Superfamily superfamilya.93.1 — Heme-dependent peroxidases
Family Family familya.93.1.1 — CCP-like
Domain ID domain_idd4jb4c_
Class classa — All alpha proteins
Fold Fold folda.93 — Heme-dependent peroxidases
Superfamily Superfamily superfamilya.93.1 — Heme-dependent peroxidases
Family Family familya.93.1.1 — CCP-like

CATH v4.4 (4 domains)

Domain ID domain_id4jb4A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id4jb4A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id4jb4C01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id4jb4C02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2

8. Citations (1)

9. Files and Curves (10)