4mu8

Crystal structure of an oxidized form of yeast iso-1-cytochrome c at pH 8.8

Method: X-RAY DIFFRACTION Dmax: 67.9 Å Quality: GOOD

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–109 Mutation:K78A, C108S HEC HEME C × 1 SO4 SULFATE ION × 4 TBU TERTIARY-BUTYL ALCOHOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.8;293 K;90% ammonia sulfate, 0.1 M Tris-HCl (pH 8.8), 4% tert-butanol, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.45 Å R-free 0.154
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–109 Mutation:K78A, C108S HEC HEME C × 1 SO4 SULFATE ION × 4 TBU TERTIARY-BUTYL ALCOHOL × 2 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.8;293 K;90% ammonia sulfate, 0.1 M Tris-HCl (pH 8.8), 4% tert-butanol, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.45 Å R-free 0.154

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–108; UniProt 2–109 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 4mu8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4mu8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4mu8
Deposition date deposition_date2013-09-20
Structure title titleCrystal structure of an oxidized form of yeast iso-1-cytochrome c at pH 8.8
Keywords keywords;oxidized form at pH 8.8, All alpha proteins, cytochrome C, electron carrier, Peroxidase Activity, HEME Binding, mitochondria, ELECTRON TRANSPORT ;; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.45
Radius of gyration Rg (electron density) rg_electron19.72
Forward intensity I(0) i012805100.00
Molecular weight molecular_weight26053.0 kDa
Excluded volume excluded_volume32250 ų
Envelope volume envelope_volume38219 ų
Hydration-shell volume shell_volume16743 ų
Envelope diameter envelope_diameter67.1
Shell Rg shell_rg25.06
Envelope Rg envelope_rg19.78
Shape Rg shape_rg19.61
Total Rg total_rg20.81
Total atoms total_atoms3443
Residues n_residues214
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 dmax67.9
Rg (real space) rg_real20.47
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.2810e+07
I(0) uncertainty (real space) i0_real_error1.7030e+05
Rg (reciprocal space) rg_reciprocal20.47
I(0) (reciprocal space) i0_reciprocal12810000.0000
Solution quality estimate total_estimate0.8809
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.4
Skewness Skewness skewness0.337
Kurtosis Kurtosis kurtosis-0.526
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3238000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4mu8a_
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_idd4mu8b_
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 (2 domains)

Domain ID domain_id4mu8A00
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_id4mu8B00
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)