5cig

Complex of yeast cytochrome c peroxidase (W191G) with iso-1 cytochrome c

Method: X-RAY DIFFRACTION Dmax: 98.5 Å Quality: EXCELLENT

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 Fragment:UNP residues 68-361 Mutation:W191G Cytochrome c iso-1 × 1 (P00044) HEC HEME C × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;PEG 3350 15-15%, 100 mM NaAcetate, 175 mM NaCl Resolution 2.06 Å R-free 0.298
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 68–361 Fragment:UNP residues 68-361 Mutation:W191G Cytochrome c iso-1 × 1 (P00044) HEC HEME C × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;PEG 3350 15-15%, 100 mM NaAcetate, 175 mM NaCl Resolution 2.06 Å R-free 0.298

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 2–109 Not recorded Cytochrome c peroxidase, mitochondrial × 1 (P00431) HEC HEME C × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;PEG 3350 15-15%, 100 mM NaAcetate, 175 mM NaCl Resolution 2.06 Å R-free 0.298
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2–109 Not recorded Cytochrome c peroxidase, mitochondrial × 1 (P00431) HEC HEME C × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;PEG 3350 15-15%, 100 mM NaAcetate, 175 mM NaCl Resolution 2.06 Å R-free 0.298

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 1–108; UniProt 2–109 Author chain D; PDBConstruct 1–108; UniProt 2–109

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 5cig

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5cig
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5cig
Deposition date deposition_date2015-07-12
Structure title titleComplex of yeast cytochrome c peroxidase (W191G) with iso-1 cytochrome c
Keywords keywords;electron transfer, heme proteins, electron hopping, multi-step tunneling, photochemistry, ELECTRON TRANSPORT-OXIDOREDUCTASE complex, ELECTRON TRANSPORT-OXIDOREDUCTASE ;; ELECTRON TRANSPORT-OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.83
Radius of gyration Rg (electron density) rg_electron29.92
Forward intensity I(0) i0137270000.00
Molecular weight molecular_weight93284.0 kDa
Excluded volume excluded_volume116600 ų
Envelope volume envelope_volume140590 ų
Hydration-shell volume shell_volume39103 ų
Envelope diameter envelope_diameter99.8
Shell Rg shell_rg37.20
Envelope Rg envelope_rg29.81
Shape Rg shape_rg29.92
Total Rg total_rg30.57
Total atoms total_atoms6588
Residues n_residues804
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 dmax98.5
Rg (real space) rg_real30.78
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.3730e+08
I(0) uncertainty (real space) i0_real_error2.2880e+06
Rg (reciprocal space) rg_reciprocal30.80
I(0) (reciprocal space) i0_reciprocal137300000.0000
Solution quality estimate total_estimate0.9019
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29820000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5ciga_
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_idd5cigb_
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_idd5cigc_
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_idd5cigd_
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 (6 domains)

Domain ID domain_id5cigA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id5cigA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id5cigB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain
Domain ID domain_id5cigC01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id5cigC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id5cigD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain

8. Citations (1)

9. Files and Curves (10)