6oua

Cryo-EM structure of the yeast Ctf3 complex

Method: ELECTRON MICROSCOPY Dmax: 101.3 Å Quality: GOOD

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

Inner kinetochore subunit CTF3

Saccharomyces cerevisiae

UniProt Q12748

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain I; UniProt 1–733 Not recorded Inner kinetochore subunit MCM16 × 1 (Q12262) Inner kinetochore subunit MCM22 × 1 (P47167) ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPI_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain I; PDBConstruct 4–736; UniProt 1–733

Inner kinetochore subunit MCM16

Saccharomyces cerevisiae

UniProt Q12262

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 1–181 Not recorded Inner kinetochore subunit CTF3 × 1 (Q12748) Inner kinetochore subunit MCM22 × 1 (P47167) ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPH_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 4–184; UniProt 1–181

Inner kinetochore subunit MCM22

Saccharomyces cerevisiae

UniProt P47167

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain K; UniProt 1–239 Not recorded Inner kinetochore subunit CTF3 × 1 (Q12748) Inner kinetochore subunit MCM16 × 1 (Q12262) ELECTRON MICROSCOPY cryo-EM buffer:pH 8.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.18 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPK_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 4–242; UniProt 1–239

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 6oua

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6oua
Deposition date deposition_date2019-05-04
Structure title titleCryo-EM structure of the yeast Ctf3 complex
Keywords keywordskinetochore, chromosome, cryo-em, CELL CYCLE; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.88
Radius of gyration Rg (electron density) rg_electron29.20
Forward intensity I(0) i083310000.00
Molecular weight molecular_weight74007.0 kDa
Excluded volume excluded_volume93835 ų
Envelope volume envelope_volume125130 ų
Hydration-shell volume shell_volume36353 ų
Envelope diameter envelope_diameter106.2
Shell Rg shell_rg35.74
Envelope Rg envelope_rg29.58
Shape Rg shape_rg29.18
Total Rg total_rg29.91
Total atoms total_atoms5208
Residues n_residues637
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 dmax101.3
Rg (real space) rg_real29.92
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real8.3310e+07
I(0) uncertainty (real space) i0_real_error1.2730e+06
Rg (reciprocal space) rg_reciprocal29.91
I(0) (reciprocal space) i0_reciprocal83310000.0000
Solution quality estimate total_estimate0.8717
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.4
Skewness Skewness skewness0.434
Kurtosis Kurtosis kurtosis-0.177
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25360000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)