2n18

Dominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase

Method: SOLUTION NMR Dmax: 83.0 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 68–361 Fragment:UNP residues 68-361 Mutation:C128A, V197C Cytochrome c iso-1 × 1 (P00044) Cytochrome c iso-1 × 1 (P00044) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEC HEME C × 2 SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 15;Pressure ambient NMR sample composition:0.4 mM [U-2H; U-15N] CcP, 0.4 mM Cc, 0.4 mM Cc1, 20 mM sodium phosphate, 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 3–109 Chain C; UniProt 2–109 Fragment:UNP residues 3-109 Mutation:A81C, C102T Fragment:UNP residues 2-109 Cytochrome c peroxidase, mitochondrial × 1 (P00431) HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEC HEME C × 2 SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 15;Pressure ambient NMR sample composition:0.4 mM [U-2H; U-15N] CcP, 0.4 mM Cc, 0.4 mM Cc1, 20 mM sodium phosphate, 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, 3
Chains and sequence ranges Author chain B; PDBConstruct 2–108; UniProt 3–109 Author chain C; 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 2n18

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n18
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n18
Deposition date deposition_date2015-03-24
Structure title titleDominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase
Keywords keywordscytochrome c, cytochrome c peroxidase, low affinity complex, 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_guinier26.55
Radius of gyration Rg (electron density) rg_electron26.44
Forward intensity I(0) i010817300000.00
Molecular weight molecular_weight891950.0 kDa
Excluded volume excluded_volume1114900 ų
Envelope volume envelope_volume93363 ų
Hydration-shell volume shell_volume29744 ų
Envelope diameter envelope_diameter89.4
Shell Rg shell_rg33.49
Envelope Rg envelope_rg27.19
Shape Rg shape_rg26.42
Total Rg total_rg26.58
Total atoms total_atoms123615
Residues n_residues7650
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 dmax83.0
Rg (real space) rg_real26.54
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.0820e+10
I(0) uncertainty (real space) i0_real_error1.2430e+08
Rg (reciprocal space) rg_reciprocal26.55
I(0) (reciprocal space) i0_reciprocal10820000000.0000
Solution quality estimate total_estimate0.8334
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.645
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8336000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2n18a_
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_idd2n18b1
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_idd2n18b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2n18c_
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_id2n18A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology520 — Peroxidase; domain 1
Homologous superfamily homologous superfamily10
Domain ID domain_id2n18A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology420 — Peroxidase; domain 2
Homologous superfamily homologous superfamily10 — Peroxidase, domain 2
Domain ID domain_id2n18B00
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_id2n18C00
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)