6gyu

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

Method: ELECTRON MICROSCOPY Dmax: 169.2 Å Quality: GOOD

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

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–608 Chain C; UniProt 49–608 Not recorded Centromere DNA-binding protein complex CBF3 subunit C × 1 (P35203) Suppressor of kinetochore protein 1 × 1 (P52286) Centromere DNA-binding protein complex CBF3 subunit A × 1 (P32504) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 1, 3
Chains and sequence ranges Author chain B; PDBConstruct 1–608; UniProt 1–608 Author chain C; PDBConstruct 5–564; UniProt 49–608

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–478 Not recorded Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) Suppressor of kinetochore protein 1 × 1 (P52286) Centromere DNA-binding protein complex CBF3 subunit A × 1 (P32504) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–478; UniProt 1–478

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–194 Not recorded Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) Centromere DNA-binding protein complex CBF3 subunit C × 1 (P35203) Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) Centromere DNA-binding protein complex CBF3 subunit A × 1 (P32504) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–194; UniProt 1–194

Centromere DNA-binding protein complex CBF3 subunit A

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–956 Not recorded Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) Centromere DNA-binding protein complex CBF3 subunit C × 1 (P35203) Centromere DNA-binding protein complex CBF3 subunit B × 1 (P40969) Suppressor of kinetochore protein 1 × 1 (P52286) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

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 5
Chains and sequence ranges Author chain E; 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 6gyu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6gyu
Deposition date deposition_date2018-07-02
Structure title titleCryo-EM structure of the CBF3-msk 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_guinier49.08
Radius of gyration Rg (electron density) rg_electron49.09
Forward intensity I(0) i0887694000.00
Molecular weight molecular_weight257220.0 kDa
Excluded volume excluded_volume325780 ų
Envelope volume envelope_volume450710 ų
Hydration-shell volume shell_volume79030 ų
Envelope diameter envelope_diameter169.1
Shell Rg shell_rg51.34
Envelope Rg envelope_rg48.14
Shape Rg shape_rg49.13
Total Rg total_rg49.05
Total atoms total_atoms18159
Residues n_residues2193
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 dmax169.2
Rg (real space) rg_real49.41
Rg uncertainty (real space) rg_real_error1.58
I(0) (real space) i0_real8.8770e+08
I(0) uncertainty (real space) i0_real_error1.9000e+07
Rg (reciprocal space) rg_reciprocal49.08
I(0) (reciprocal space) i0_reciprocal887300000.0000
Solution quality estimate total_estimate0.8466
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.6
Skewness Skewness skewness0.472
Kurtosis Kurtosis kurtosis-0.360
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha149300000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.640

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6gyuD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology710 — Potassium Channel Kv1.1; Chain A
Homologous superfamily homologous superfamily10 — Potassium Channel Kv1.1; Chain A
Domain ID domain_id6gyuE02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology443 — hpI Integrase; Chain A
Homologous superfamily homologous superfamily20 — Centromere DNA-binding protein complex CBF3 subunit, domain 2

8. Citations (1)

9. Files and Curves (10)