4geq

Crystal structure of the Spc24-Spc25/Cnn1 binding interface

Method: X-RAY DIFFRACTION Dmax: 71.9 Å Quality: EXCELLENT

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

Kinetochore protein SPC25

Saccharomyces cerevisiae S288c

UniProt P40014

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 133–221 Fragment:Spc25p C-terminal domain, residues 133-221 Kinetochore protein SPC24 × 1 (Q04477) Kinetochore-associated protein CNN1 × 1 (P43618) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.6;293.15 K;15% PEG6000, 5% glycerol; Drop volume: 0.2ul; Protein proportion: 50%; Protein concentration: 6 mg/ml, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.01 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 133–221 Fragment:Spc25p C-terminal domain, residues 133-221 Kinetochore protein SPC24 × 1 (Q04477) Kinetochore-associated protein CNN1 × 1 (P43618) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.6;293.15 K;15% PEG6000, 5% glycerol; Drop volume: 0.2ul; Protein proportion: 50%; Protein concentration: 6 mg/ml, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.01 Å R-free 0.258

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPC25_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–90; UniProt 133–221 Author chain C; PDBConstruct 2–90; UniProt 133–221

Kinetochore protein SPC24

Saccharomyces cerevisiae S288c

UniProt Q04477

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 155–213 Fragment:Spc24p C-terminal domain, residues 155-213 Kinetochore protein SPC25 × 1 (P40014) Kinetochore-associated protein CNN1 × 1 (P43618) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.6;293.15 K;15% PEG6000, 5% glycerol; Drop volume: 0.2ul; Protein proportion: 50%; Protein concentration: 6 mg/ml, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.01 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 155–213 Fragment:Spc24p C-terminal domain, residues 155-213 Kinetochore protein SPC25 × 1 (P40014) Kinetochore-associated protein CNN1 × 1 (P43618) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.6;293.15 K;15% PEG6000, 5% glycerol; Drop volume: 0.2ul; Protein proportion: 50%; Protein concentration: 6 mg/ml, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.01 Å R-free 0.258

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPC24_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–60; UniProt 155–213 Author chain D; PDBConstruct 2–60; UniProt 155–213

Kinetochore-associated protein CNN1

OrganismNot specified

UniProt P43618

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 F; UniProt 60–84 Fragment:Cnn1p N-terminal motif, residues 60-84 Kinetochore protein SPC25 × 1 (P40014) Kinetochore protein SPC24 × 1 (Q04477) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.6;293.15 K;15% PEG6000, 5% glycerol; Drop volume: 0.2ul; Protein proportion: 50%; Protein concentration: 6 mg/ml, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.01 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 60–84 Fragment:Cnn1p N-terminal motif, residues 60-84 Kinetochore protein SPC25 × 1 (P40014) Kinetochore protein SPC24 × 1 (Q04477) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.6;293.15 K;15% PEG6000, 5% glycerol; Drop volume: 0.2ul; Protein proportion: 50%; Protein concentration: 6 mg/ml, pH 7.6, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K Resolution 2.01 Å R-free 0.258

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 CNN1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–25; UniProt 60–84 Author chain F; PDBConstruct 1–25; UniProt 60–84

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 4geq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4geq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4geq
Deposition date deposition_date2012-08-02
Structure title titleCrystal structure of the Spc24-Spc25/Cnn1 binding interface
Keywords keywordsprotein-protein complex, Ndc80-binding motif, RWD domain, kinetochore components, nucleus, 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_guinier23.19
Radius of gyration Rg (electron density) rg_electron21.97
Forward intensity I(0) i023064300.00
Molecular weight molecular_weight36778.0 kDa
Excluded volume excluded_volume46202 ų
Envelope volume envelope_volume57182 ų
Hydration-shell volume shell_volume22025 ų
Envelope diameter envelope_diameter71.8
Shell Rg shell_rg28.23
Envelope Rg envelope_rg21.81
Shape Rg shape_rg21.97
Total Rg total_rg22.79
Total atoms total_atoms2594
Residues n_residues331
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 dmax71.9
Rg (real space) rg_real23.12
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.3060e+07
I(0) uncertainty (real space) i0_real_error2.9940e+05
Rg (reciprocal space) rg_reciprocal23.14
I(0) (reciprocal space) i0_reciprocal23060000.0000
Solution quality estimate total_estimate0.9109
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.222
Kurtosis Kurtosis kurtosis-0.510
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3580000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4geqA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology457 — Copper Amine Oxidase; Chain A, domain 1
Homologous superfamily homologous superfamily50 — Chromosome segregation protein Spc25
Domain ID domain_id4geqB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily430
Domain ID domain_id4geqC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology457 — Copper Amine Oxidase; Chain A, domain 1
Homologous superfamily homologous superfamily50 — Chromosome segregation protein Spc25
Domain ID domain_id4geqD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily430

8. Citations (1)

9. Files and Curves (10)