7k79

CBF3

Method: ELECTRON MICROSCOPY Dmax: 124.9 Å Quality: REASONABLE

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

Centromere DNA-binding protein complex CBF3 subunit C

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P35203

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain K; UniProt 2–478 Not recorded Centromere DNA-binding protein complex CBF3 subunit B × 2 (P40969) Suppressor of kinetochore protein 1 × 1 (P52286) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBF3C_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 3–479; UniProt 2–478

Centromere DNA-binding protein complex CBF3 subunit B

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P40969

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain L; UniProt 1–608 Chain O; UniProt 1–608 Not recorded Centromere DNA-binding protein complex CBF3 subunit C × 1 (P35203) Suppressor of kinetochore protein 1 × 1 (P52286) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBF3B_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–608; UniProt 1–608 Author chain O; PDBConstruct 1–608; UniProt 1–608

Suppressor of kinetochore protein 1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P52286

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain N; UniProt 1–194 Not recorded Centromere DNA-binding protein complex CBF3 subunit C × 1 (P35203) Centromere DNA-binding protein complex CBF3 subunit B × 2 (P40969) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

13 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SKP1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 1–194; UniProt 1–194

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 7k79

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7k79
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7k79
Deposition date deposition_date2020-09-22
Structure title titleCBF3
Keywords keywordsCBF3, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.29
Radius of gyration Rg (electron density) rg_electron38.51
Forward intensity I(0) i0481057000.00
Molecular weight molecular_weight187940.0 kDa
Excluded volume excluded_volume238800 ų
Envelope volume envelope_volume325260 ų
Hydration-shell volume shell_volume67806 ų
Envelope diameter envelope_diameter135.2
Shell Rg shell_rg46.63
Envelope Rg envelope_rg37.85
Shape Rg shape_rg38.52
Total Rg total_rg38.98
Total atoms total_atoms13272
Residues n_residues1601
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 dmax124.9
Rg (real space) rg_real39.09
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real4.8110e+08
I(0) uncertainty (real space) i0_real_error7.8670e+06
Rg (reciprocal space) rg_reciprocal39.22
I(0) (reciprocal space) i0_reciprocal481100000.0000
Solution quality estimate total_estimate0.6709
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.0
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-0.477
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha137200000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 0.992; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)