1dsg

CYTOCHROME C PEROXIDASE H175G MUTANT, IMIDAZOLE COMPLEX AT PH 5, ROOM TEMPERATURE.

Method: X-RAY DIFFRACTION Dmax: 61.1 Å Quality: GOOD

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

CYTOCHROME C PEROXIDASE

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 70–361 Mutation:H175G HEM PROTOPORPHYRIN IX CONTAINING FE × 1 IMD IMIDAZOLE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICRODIALYSIS;pH 5.2;288 K;MES, imidazole, pH 5.2, MICRODIALYSIS, temperature 288K Resolution 2.56 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.

175 other PDB entries and 193 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 1–292; UniProt 70–361

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 1dsg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dsg
Deposition date deposition_date2000-01-07
Structure title titleCYTOCHROME C PEROXIDASE H175G MUTANT, IMIDAZOLE COMPLEX AT PH 5, ROOM TEMPERATURE.
Keywords keywordsheme enzyme, peroxidase, cavity mutant, ligand binding, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.49
Radius of gyration Rg (electron density) rg_electron18.41
Forward intensity I(0) i019462100.00
Molecular weight molecular_weight33747.0 kDa
Excluded volume excluded_volume42167 ų
Envelope volume envelope_volume46240 ų
Hydration-shell volume shell_volume20605 ų
Envelope diameter envelope_diameter64.9
Shell Rg shell_rg25.10
Envelope Rg envelope_rg18.64
Shape Rg shape_rg18.39
Total Rg total_rg19.39
Total atoms total_atoms2390
Residues n_residues291
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 dmax61.1
Rg (real space) rg_real19.35
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real1.9460e+07
I(0) uncertainty (real space) i0_real_error2.2660e+05
Rg (reciprocal space) rg_reciprocal19.37
I(0) (reciprocal space) i0_reciprocal19460000.0000
Solution quality estimate total_estimate0.8158
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.133
Kurtosis Kurtosis kurtosis-0.398
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5439000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1dsga_
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 (2 domains)

Domain ID domain_id1dsgA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id1dsgA02
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)