6h08

The crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae with a His175Me-His proximal ligand substitution

Method: X-RAY DIFFRACTION Dmax: 112.2 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 71–361 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CO COBALT (II) ION × 1 MN MANGANESE (II) ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;5 mM cobalt(II) chloride hexahydrate, 5 mM cadmium chloride hemi(pentahydrate), 5 mM magnesium chloride hexahydrate, 5 mM nickel(II) chloride hexahydrate, 0.1 M HEPES pH 7.5 and 12% w/v PEG 3350 Resolution 1.90 Å R-free 0.205
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 71–361 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CO COBALT (II) ION × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;5 mM cobalt(II) chloride hexahydrate, 5 mM cadmium chloride hemi(pentahydrate), 5 mM magnesium chloride hexahydrate, 5 mM nickel(II) chloride hexahydrate, 0.1 M HEPES pH 7.5 and 12% w/v PEG 3350 Resolution 1.90 Å R-free 0.205
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 71–361 Non-standard monomer:Yes (specific site not provided by mmCIF) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CO COBALT (II) ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;277 K;5 mM cobalt(II) chloride hexahydrate, 5 mM cadmium chloride hemi(pentahydrate), 5 mM magnesium chloride hexahydrate, 5 mM nickel(II) chloride hexahydrate, 0.1 M HEPES pH 7.5 and 12% w/v PEG 3350 Resolution 1.90 Å R-free 0.205

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 191 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 7–297; UniProt 71–361 Author chain B; PDBConstruct 7–297; UniProt 71–361 Author chain C; PDBConstruct 7–297; UniProt 71–361

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 6h08

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6h08
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6h08
Deposition date deposition_date2018-07-06
Structure title titleThe crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae with a His175Me-His proximal ligand substitution
Keywords keywordsEngineered cytochrome c peroxidase, Saccharomyces cerevisiae, Me-His, proximal ligand, oxidoreductase; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.28
Radius of gyration Rg (electron density) rg_electron31.45
Forward intensity I(0) i0172905000.00
Molecular weight molecular_weight104210.0 kDa
Excluded volume excluded_volume129530 ų
Envelope volume envelope_volume160430 ų
Hydration-shell volume shell_volume42125 ų
Envelope diameter envelope_diameter115.4
Shell Rg shell_rg38.82
Envelope Rg envelope_rg31.38
Shape Rg shape_rg31.43
Total Rg total_rg32.10
Total atoms total_atoms7360
Residues n_residues886
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 dmax112.2
Rg (real space) rg_real32.21
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real1.7290e+08
I(0) uncertainty (real space) i0_real_error2.7330e+06
Rg (reciprocal space) rg_reciprocal32.25
I(0) (reciprocal space) i0_reciprocal172900000.0000
Solution quality estimate total_estimate0.8784
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.6
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.464
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41070000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.816; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd6h08a1
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_idd6h08a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6h08b1
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_idd6h08b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6h08c1
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_idd6h08c2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id6h08C01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id6h08C02
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)