6gsa

Core Centromere Binding Factor 3 (CBF3) with monomeric Ndc10

Method: ELECTRON MICROSCOPY Dmax: 174.6 Å Quality: GOOD

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

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 heterocomplex Heteromer Protein × 5 PDB declaration: tetrameric(4) Count mismatch; review required Chain A; UniProt 47–608 Chain B; UniProt 47–608 Mutation:Truncation of the N-terminal domain, UNP residues 1-46 Suppressor of kinetochore protein 1 × 1 (P52286) Centromere DNA-binding protein complex CBF3 subunit C × 1 (P35203) Centromere DNA-binding protein complex CBF3 subunit A × 1 (P32504) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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
Chains and sequence ranges Author chain A; PDBConstruct 23–584; UniProt 47–608 Author chain B; PDBConstruct 23–584; UniProt 47–608

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 heterocomplex Heteromer Protein × 5 PDB declaration: tetrameric(4) Count mismatch; review required Chain C; UniProt 2–194 Not recorded Centromere DNA-binding protein complex CBF3 subunit B × 2 (P40969) Centromere DNA-binding protein complex CBF3 subunit C × 1 (P35203) Centromere DNA-binding protein complex CBF3 subunit A × 1 (P32504) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 2
Chains and sequence ranges Author chain C; PDBConstruct 3–195; UniProt 2–194

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 heterocomplex Heteromer Protein × 5 PDB declaration: tetrameric(4) Count mismatch; review required Chain D; UniProt 2–478 Not recorded Centromere DNA-binding protein complex CBF3 subunit B × 2 (P40969) Suppressor of kinetochore protein 1 × 1 (P52286) Centromere DNA-binding protein complex CBF3 subunit A × 1 (P32504) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 3
Chains and sequence ranges Author chain D; PDBConstruct 3–479; UniProt 2–478

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 heterocomplex Heteromer Protein × 5 PDB declaration: tetrameric(4) Count mismatch; review required Chain E; UniProt 2–553 Fragment:UNP residues 2-553 Mutation:Construct comprising residues 1-554 with C-terminal Strep tag Centromere DNA-binding protein complex CBF3 subunit B × 2 (P40969) Suppressor of kinetochore protein 1 × 1 (P52286) Centromere DNA-binding protein complex CBF3 subunit C × 1 (P35203) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.20 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 3–554; UniProt 2–553

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 6gsa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6gsa
Deposition date deposition_date2018-06-13
Structure title titleCore Centromere Binding Factor 3 (CBF3) with monomeric Ndc10
Keywords keywordsCentromere, CDEIII-binding, LRR domain, 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_guinier50.42
Radius of gyration Rg (electron density) rg_electron50.32
Forward intensity I(0) i0697342000.00
Molecular weight molecular_weight230080.0 kDa
Excluded volume excluded_volume292300 ų
Envelope volume envelope_volume421650 ų
Hydration-shell volume shell_volume74100 ų
Envelope diameter envelope_diameter171.6
Shell Rg shell_rg50.81
Envelope Rg envelope_rg48.95
Shape Rg shape_rg50.35
Total Rg total_rg50.22
Total atoms total_atoms16272
Residues n_residues1999
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 dmax174.6
Rg (real space) rg_real50.68
Rg uncertainty (real space) rg_real_error2.08
I(0) (real space) i0_real6.9730e+08
I(0) uncertainty (real space) i0_real_error1.4290e+07
Rg (reciprocal space) rg_reciprocal50.19
I(0) (reciprocal space) i0_reciprocal696900000.0000
Solution quality estimate total_estimate0.7750
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.7
Skewness Skewness skewness0.479
Kurtosis Kurtosis kurtosis-0.480
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha78080000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.747; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.830; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)