6rsk

Cytochrome c co-crystallized with 20 eq. sulfonato-calix[8]arene and 15 eq. spermine - structure II

Method: X-RAY DIFFRACTION Dmax: 87.1 Å Quality: REASONABLE

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

Cytochrome c iso-1

Saccharomyces cerevisiae S288c

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 3–109 Not recorded HEC HEME C × 1 EVB sulfonato-calix[8]arene × 3 SO4 SULFATE ION × 6 SPM SPERMINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M HEPES pH 7.5, 0.15 M NaCl, 2.2 M Ammonium sulfate, 0.04 M sulfonato-calix[8]arene, 0.03 M spermine Resolution 2.31 Å R-free 0.222
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3–109 Not recorded HEC HEME C × 1 EVB sulfonato-calix[8]arene × 3 SO4 SULFATE ION × 5 SPM SPERMINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M HEPES pH 7.5, 0.15 M NaCl, 2.2 M Ammonium sulfate, 0.04 M sulfonato-calix[8]arene, 0.03 M spermine Resolution 2.31 Å R-free 0.222

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 2–108; UniProt 3–109 Author chain B; PDBConstruct 2–108; UniProt 3–109

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 6rsk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6rsk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6rsk
Deposition date deposition_date2019-05-21
Structure title titleCytochrome c co-crystallized with 20 eq. sulfonato-calix[8]arene and 15 eq. spermine - structure II
Keywords keywordsMolecular glues, Molecular switch, spermine, polyamine, calixarene, supramolecular chemistry, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.71
Radius of gyration Rg (electron density) rg_electron24.17
Forward intensity I(0) i026832900.00
Molecular weight molecular_weight36093.0 kDa
Excluded volume excluded_volume43308 ų
Envelope volume envelope_volume55017 ų
Hydration-shell volume shell_volume20192 ų
Envelope diameter envelope_diameter89.0
Shell Rg shell_rg29.40
Envelope Rg envelope_rg24.24
Shape Rg shape_rg24.13
Total Rg total_rg24.89
Total atoms total_atoms2465
Residues n_residues216
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 dmax87.1
Rg (real space) rg_real24.92
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real2.6830e+07
I(0) uncertainty (real space) i0_real_error3.6730e+05
Rg (reciprocal space) rg_reciprocal24.87
I(0) (reciprocal space) i0_reciprocal26830000.0000
Solution quality estimate total_estimate0.6190
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.491
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10150000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.628; Stabil: 1.000; Sysdev: 0.184; Positv: 1.000; Valcen: 0.614; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6rska1
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_idd6rska2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6rskb1
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_idd6rskb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)