1cty

MUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT

Method: X-RAY DIFFRACTION Dmax: 45.0 Å Quality: GOOD

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

CYTOCHROME C

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 1–108 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 HEC HEME C × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å

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 1
Chains and sequence ranges Author chain A; 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 1cty

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cty
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cty
Deposition date deposition_date1993-02-15
Structure title titleMUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT
Keywords keywordsELECTRON TRANSPORT (HEME PROTEIN); ELECTRON TRANSPORT (HEME PROTEIN)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.22
Radius of gyration Rg (electron density) rg_electron12.89
Forward intensity I(0) i03322880.00
Molecular weight molecular_weight12799.0 kDa
Excluded volume excluded_volume16039 ų
Envelope volume envelope_volume17371 ų
Hydration-shell volume shell_volume11324 ų
Envelope diameter envelope_diameter45.2
Shell Rg shell_rg18.85
Envelope Rg envelope_rg13.37
Shape Rg shape_rg12.83
Total Rg total_rg14.37
Total atoms total_atoms898
Residues n_residues107
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 dmax45.0
Rg (real space) rg_real14.11
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real3.3230e+06
I(0) uncertainty (real space) i0_real_error3.4040e+04
Rg (reciprocal space) rg_reciprocal14.12
I(0) (reciprocal space) i0_reciprocal3323000.0000
Solution quality estimate total_estimate0.8053
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.8
Skewness Skewness skewness0.133
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha631800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ctya_
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 (1 domains)

Domain ID domain_id1ctyA00
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 (7)

9. Files and Curves (10)