8t0p

Structure of Cse4 bound to Ame1 and Okp1

Method: X-RAY DIFFRACTION Dmax: 103.9 Å Quality: REASONABLE

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

Inner kinetochore subunit AME1

Saccharomyces cerevisiae

UniProt P38313

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 B; UniProt 125–231 Fragment:residues 125-231 Inner kinetochore subunit OKP1 × 1 (P53298) Histone H3-like centromeric protein CSE4 × 1 (P36012) SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;19% PEG 8000, 0.55 M Lithium sulfate Resolution 1.73 Å R-free 0.236

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 CENPU_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–107; UniProt 125–231

Inner kinetochore subunit OKP1

Saccharomyces cerevisiae

UniProt P53298

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 A; UniProt 125–275 Fragment:residues 125-275 Inner kinetochore subunit AME1 × 1 (P38313) Histone H3-like centromeric protein CSE4 × 1 (P36012) SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;19% PEG 8000, 0.55 M Lithium sulfate Resolution 1.73 Å R-free 0.236

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 CENPQ_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 2–152; UniProt 125–275

Histone H3-like centromeric protein CSE4

OrganismNot specified

UniProt P36012

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 C; UniProt 32–49 Fragment:residues 32-49 Inner kinetochore subunit AME1 × 1 (P38313) Inner kinetochore subunit OKP1 × 1 (P53298) SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;19% PEG 8000, 0.55 M Lithium sulfate Resolution 1.73 Å R-free 0.236

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CENPA_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–18; UniProt 32–49

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 8t0p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t0p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t0p
Deposition date deposition_date2023-06-01
Structure title titleStructure of Cse4 bound to Ame1 and Okp1
Keywords keywordsOkp1, Cse4, Ame1, Kinetochore, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.53
Radius of gyration Rg (electron density) rg_electron27.63
Forward intensity I(0) i019103600.00
Molecular weight molecular_weight32839.0 kDa
Excluded volume excluded_volume40966 ų
Envelope volume envelope_volume52441 ų
Hydration-shell volume shell_volume18922 ų
Envelope diameter envelope_diameter110.2
Shell Rg shell_rg29.23
Envelope Rg envelope_rg28.91
Shape Rg shape_rg27.64
Total Rg total_rg27.77
Total atoms total_atoms2302
Residues n_residues277
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 dmax103.9
Rg (real space) rg_real28.19
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real1.9100e+07
I(0) uncertainty (real space) i0_real_error3.0320e+05
Rg (reciprocal space) rg_reciprocal27.98
I(0) (reciprocal space) i0_reciprocal19100000.0000
Solution quality estimate total_estimate0.7327
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.793
Kurtosis Kurtosis kurtosis0.238
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2229000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.486; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.312; Smooth: 0.751

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)