2jti

Solution structure of the yeast iso-1-cytochrome c (T12A) : yeast cytochrome c peroxidase complex

Method: SOLUTION NMR Dmax: 72.8 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:N38C,N200C,S263C,T288C,C128A Cytochrome c iso-1 × 1 (P00044) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEC HEME C × 1 SOLUTION NMR NMR measurement conditions:pH 6;303 K;Pressure ambient NMR sample composition:0.3-0.4 mM [U-15N] CC, 0.3-0.4 mM CCP, 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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 1–294; 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 2–109 Mutation:T12A,C102T Cytochrome c peroxidase, mitochondrial × 1 (P00431) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEC HEME C × 1 SOLUTION NMR NMR measurement conditions:pH 6;303 K;Pressure ambient NMR sample composition:0.3-0.4 mM [U-15N] CC, 0.3-0.4 mM CCP, 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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 125 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

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 2jti

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jti
Deposition date deposition_date2007-08-01
Structure title titleSolution structure of the yeast iso-1-cytochrome c (T12A) : yeast cytochrome c peroxidase complex
Keywords keywords;protein/protein, Heme, Hydrogen peroxide, Iron, Metal-binding, Mitochondrion, Oxidoreductase, Peroxidase, Transit peptide, Electron transport, Methylation, Respiratory chain, Transport, OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX ;; OXIDOREDUCTASE/ELECTRON TRANSPORT
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier22.16
Radius of gyration Rg (electron density) rg_electron21.82
Forward intensity I(0) i02917830000.00
Molecular weight molecular_weight461630.0 kDa
Excluded volume excluded_volume577040 ų
Envelope volume envelope_volume69689 ų
Hydration-shell volume shell_volume26080 ų
Envelope diameter envelope_diameter79.0
Shell Rg shell_rg29.36
Envelope Rg envelope_rg22.32
Shape Rg shape_rg21.79
Total Rg total_rg22.02
Total atoms total_atoms63780
Residues n_residues3970
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 dmax72.8
Rg (real space) rg_real22.09
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real2.9180e+09
I(0) uncertainty (real space) i0_real_error3.4450e+07
Rg (reciprocal space) rg_reciprocal22.11
I(0) (reciprocal space) i0_reciprocal2918000000.0000
Solution quality estimate total_estimate0.8895
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.1
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.333
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha6521000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2jtia_
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_idd2jtib_
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 (3 domains)

Domain ID domain_id2jtiA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id2jtiA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id2jtiB00
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)