2b11

Crystal structure of the protein-protein complex between F82W cytochrome c and cytochrome c peroxidase

Method: X-RAY DIFFRACTION Dmax: 116.4 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 68–361 Mutation:F82W Cytochrome c iso-1 × 1 (P00044) ZNH PROTOPORPHYRIN IX CONTAINING ZN × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;PEG 3350, NaCl, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.30 Å R-free 0.293
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 68–361 Mutation:F82W Cytochrome c iso-1 × 1 (P00044) HEC HEME C × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;PEG 3350, NaCl, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.30 Å R-free 0.293

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

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 1–108 Mutation:F82W Cytochrome c peroxidase, mitochondrial × 1 (P00431) ZNH PROTOPORPHYRIN IX CONTAINING ZN × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;PEG 3350, NaCl, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.30 Å R-free 0.293
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–108 Mutation:F82W Cytochrome c peroxidase, mitochondrial × 1 (P00431) HEC HEME C × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;PEG 3350, NaCl, pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.30 Å R-free 0.293

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

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 2b11

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2b11
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2b11
Deposition date deposition_date2005-09-15
Structure title titleCrystal structure of the protein-protein complex between F82W cytochrome c and cytochrome c peroxidase
Keywords keywordscytochrome, electron transfer, OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX; OXIDOREDUCTASE/ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.05
Radius of gyration Rg (electron density) rg_electron34.73
Forward intensity I(0) i0135222000.00
Molecular weight molecular_weight93609.0 kDa
Excluded volume excluded_volume116940 ų
Envelope volume envelope_volume151500 ų
Hydration-shell volume shell_volume36947 ų
Envelope diameter envelope_diameter118.7
Shell Rg shell_rg40.39
Envelope Rg envelope_rg34.33
Shape Rg shape_rg34.73
Total Rg total_rg35.13
Total atoms total_atoms6612
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 dmax116.4
Rg (real space) rg_real35.18
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.3520e+08
I(0) uncertainty (real space) i0_real_error2.4380e+06
Rg (reciprocal space) rg_reciprocal35.10
I(0) (reciprocal space) i0_reciprocal135200000.0000
Solution quality estimate total_estimate0.8780
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.1
Skewness Skewness skewness0.344
Kurtosis Kurtosis kurtosis-0.623
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22940000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.886; Smooth: 0.898

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2b11a_
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_idd2b11b1
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_idd2b11c_
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_idd2b11d_
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_id2b11A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id2b11A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id2b11B00
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_id2b11C01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id2b11C02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id2b11D00
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)