6gys

Cryo-EM structure of the CBF3-CEN3 complex of the budding yeast kinetochore

Method: ELECTRON MICROSCOPY Dmax: 218.5 Å Quality: GOOD

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

Centromere DNA-binding protein complex CBF3 subunit C

Saccharomyces cerevisiae

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–478 Chain H; UniProt 1–478 Not recorded Centromere DNA-binding protein complex CBF3 subunit B × 4 (P40969) Suppressor of kinetochore protein 1 × 2 (P52286) Centromere DNA-binding protein complex CBF3 subunit A × 2 (P32504) DNA (52-MER) × 1 DNA (52-MER) × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 A; PDBConstruct 1–478; UniProt 1–478 Author chain H; PDBConstruct 1–478; UniProt 1–478

Centromere DNA-binding protein complex CBF3 subunit B

Saccharomyces cerevisiae

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 1–608 Chain C; UniProt 1–608 Chain I; UniProt 1–608 Chain J; UniProt 1–608 Not recorded Centromere DNA-binding protein complex CBF3 subunit C × 2 (P35203) Suppressor of kinetochore protein 1 × 2 (P52286) Centromere DNA-binding protein complex CBF3 subunit A × 2 (P32504) DNA (52-MER) × 1 DNA (52-MER) × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 B; PDBConstruct 1–608; UniProt 1–608 Author chain C; PDBConstruct 1–608; UniProt 1–608 Author chain I; PDBConstruct 1–608; UniProt 1–608 Author chain J; PDBConstruct 1–608; UniProt 1–608

Suppressor of kinetochore protein 1

Saccharomyces cerevisiae

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–194 Chain K; UniProt 1–194 Not recorded Centromere DNA-binding protein complex CBF3 subunit C × 2 (P35203) Centromere DNA-binding protein complex CBF3 subunit B × 4 (P40969) Centromere DNA-binding protein complex CBF3 subunit A × 2 (P32504) DNA (52-MER) × 1 DNA (52-MER) × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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 D; PDBConstruct 1–194; UniProt 1–194 Author chain K; PDBConstruct 1–194; UniProt 1–194

Centromere DNA-binding protein complex CBF3 subunit A

Saccharomyces cerevisiae

UniProt P32504

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–DNA Heteromer Protein × 10 DNA 2 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain E; UniProt 1–956 Chain L; UniProt 1–956 Not recorded Centromere DNA-binding protein complex CBF3 subunit C × 2 (P35203) Centromere DNA-binding protein complex CBF3 subunit B × 4 (P40969) Suppressor of kinetochore protein 1 × 2 (P52286) DNA (52-MER) × 1 DNA (52-MER) × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CBF3A_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–956; UniProt 1–956 Author chain L; PDBConstruct 1–956; UniProt 1–956

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 6gys

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6gys
Deposition date deposition_date2018-07-01
Structure title titleCryo-EM structure of the CBF3-CEN3 complex of the budding yeast kinetochore
Keywords keywordsComplex, 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_guinier76.63
Radius of gyration Rg (electron density) rg_electron77.92
Forward intensity I(0) i04283110000.00
Molecular weight molecular_weight553430.0 kDa
Excluded volume excluded_volume690740 ų
Envelope volume envelope_volume1075000 ų
Hydration-shell volume shell_volume118790 ų
Envelope diameter envelope_diameter249.4
Shell Rg shell_rg72.44
Envelope Rg envelope_rg74.52
Shape Rg shape_rg77.93
Total Rg total_rg77.81
Total atoms total_atoms38890
Residues n_residues4545
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 dmax218.5
Rg (real space) rg_real76.29
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real4.2510e+09
I(0) uncertainty (real space) i0_real_error8.3020e+07
Rg (reciprocal space) rg_reciprocal74.53
I(0) (reciprocal space) i0_reciprocal4259000000.0000
Solution quality estimate total_estimate0.8308
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.6
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.772
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.1830
Highest regularization parameter α highest_alpha316300000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)