6p41

Yeast cytochrome c peroxidase (W191Y:L232E) in complex with iso-1 cytochrome c

Method: X-RAY DIFFRACTION Dmax: 116.8 Å Quality: REASONABLE

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

Cytochrome c peroxidase, mitochondrial

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 68–361 Mutation:W191Y, L232E Cytochrome c iso-1 × 1 (P00044) HEM PROTOPORPHYRIN IX CONTAINING FE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;100 mM sodium acetate,175 mM NaCl, 5 mM n-octyl-B-D-glucoside, polyethylene glycol 3350 18%-20% Resolution 2.90 Å R-free 0.273
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 68–361 Mutation:W191Y, L232E Cytochrome c iso-1 × 1 (P00044) HEM PROTOPORPHYRIN IX CONTAINING FE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;100 mM sodium acetate,175 mM NaCl, 5 mM n-octyl-B-D-glucoside, polyethylene glycol 3350 18%-20% Resolution 2.90 Å R-free 0.273

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

Cytochrome c iso-1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P00044

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 7–109 Not recorded Cytochrome c peroxidase, mitochondrial × 1 (P00431) HEM PROTOPORPHYRIN IX CONTAINING FE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;100 mM sodium acetate,175 mM NaCl, 5 mM n-octyl-B-D-glucoside, polyethylene glycol 3350 18%-20% Resolution 2.90 Å R-free 0.273
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 7–109 Not recorded Cytochrome c peroxidase, mitochondrial × 1 (P00431) HEM PROTOPORPHYRIN IX CONTAINING FE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;100 mM sodium acetate,175 mM NaCl, 5 mM n-octyl-B-D-glucoside, polyethylene glycol 3350 18%-20% Resolution 2.90 Å R-free 0.273

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.

91 other PDB entries and 124 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYC1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 7–109 Author chain D; PDBConstruct 1–103; UniProt 7–109

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 6p41

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6p41
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6p41
Deposition date deposition_date2019-05-25
Structure title titleYeast cytochrome c peroxidase (W191Y:L232E) in complex with iso-1 cytochrome c
Keywords keywordsheme proteins, electron hopping, multi-step tunneling, electron transport-oxidoreductase complex, ELECTRON TRANSPORT; Electron transport/Oxidoreductase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.85
Radius of gyration Rg (electron density) rg_electron35.49
Forward intensity I(0) i0130612000.00
Molecular weight molecular_weight92299.0 kDa
Excluded volume excluded_volume115300 ų
Envelope volume envelope_volume151530 ų
Hydration-shell volume shell_volume35737 ų
Envelope diameter envelope_diameter123.9
Shell Rg shell_rg41.69
Envelope Rg envelope_rg34.87
Shape Rg shape_rg35.49
Total Rg total_rg35.93
Total atoms total_atoms6522
Residues n_residues794
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 dmax116.8
Rg (real space) rg_real35.97
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real1.3060e+08
I(0) uncertainty (real space) i0_real_error2.1500e+06
Rg (reciprocal space) rg_reciprocal35.90
I(0) (reciprocal space) i0_reciprocal130600000.0000
Solution quality estimate total_estimate0.6664
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.774
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha22550000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 0.101; Positv: 1.000; Valcen: 0.830; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6p41a_
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_idd6p41b_
Class classa — All alpha proteins
Fold Fold folda.3 — Cytochrome c
Superfamily Superfamily superfamilya.3.1 — Cytochrome c
Family Family familya.3.1.1 — monodomain cytochrome c
Domain ID domain_idd6p41c_
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_idd6p41d_
Class classa — All alpha proteins
Fold Fold folda.3 — Cytochrome c
Superfamily Superfamily superfamilya.3.1 — Cytochrome c
Family Family familya.3.1.1 — monodomain cytochrome c

CATH v4.4 (4 domains)

Domain ID domain_id6p41A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id6p41A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id6p41C01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id6p41C02
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)