2gv5

crystal structure of Sfi1p/Cdc31p complex

Method: X-RAY DIFFRACTION Dmax: 148.2 Å Quality: GOOD

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

Cell division control protein 31

Saccharomyces cerevisiae

UniProt P06704

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 1–161 Chain B; UniProt 1–161 Non-standard monomer:Yes (specific site not provided by mmCIF) Sfi1p × 1 (Q12369) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;0.2 M sodium acetate, 18% PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.00 Å R-free 0.297
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–161 Chain E; UniProt 1–161 Non-standard monomer:Yes (specific site not provided by mmCIF) Sfi1p × 1 (Q12369) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;0.2 M sodium acetate, 18% PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.00 Å R-free 0.297

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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC31_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–161; UniProt 1–161 Author chain B; PDBConstruct 1–161; UniProt 1–161 Author chain D; PDBConstruct 1–161; UniProt 1–161 Author chain E; PDBConstruct 1–161; UniProt 1–161

Sfi1p

Saccharomyces cerevisiae

UniProt Q12369

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 643–710 Fragment:Residues: 643-710 Non-standard monomer:Yes (specific site not provided by mmCIF) Cell division control protein 31 × 2 (P06704) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;0.2 M sodium acetate, 18% PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.00 Å R-free 0.297
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 643–710 Fragment:Residues: 643-710 Non-standard monomer:Yes (specific site not provided by mmCIF) Cell division control protein 31 × 2 (P06704) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;0.2 M sodium acetate, 18% PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.00 Å R-free 0.297

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q12369_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 6–73; UniProt 643–710 Author chain F; PDBConstruct 6–73; UniProt 643–710

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 2gv5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2gv5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2gv5
Deposition date deposition_date2006-05-02
Structure title titlecrystal structure of Sfi1p/Cdc31p complex
Keywords keywordsSfi1p, centrin, cdc31p, spindle pole body, centrosome, 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_guinier40.62
Radius of gyration Rg (electron density) rg_electron41.10
Forward intensity I(0) i0125151000.00
Molecular weight molecular_weight88065.0 kDa
Excluded volume excluded_volume108940 ų
Envelope volume envelope_volume160210 ų
Hydration-shell volume shell_volume36412 ų
Envelope diameter envelope_diameter157.8
Shell Rg shell_rg40.56
Envelope Rg envelope_rg41.22
Shape Rg shape_rg41.10
Total Rg total_rg41.06
Total atoms total_atoms6122
Residues n_residues716
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 dmax148.2
Rg (real space) rg_real41.04
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real1.2520e+08
I(0) uncertainty (real space) i0_real_error2.2430e+06
Rg (reciprocal space) rg_reciprocal40.62
I(0) (reciprocal space) i0_reciprocal125100000.0000
Solution quality estimate total_estimate0.7808
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary45.6
Skewness Skewness skewness0.669
Kurtosis Kurtosis kurtosis0.322
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4679000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.646; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.721; Smooth: 0.485

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2gv5a_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.0 — automated matches
Domain ID domain_idd2gv5b_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.0 — automated matches
Domain ID domain_idd2gv5d_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.0 — automated matches
Domain ID domain_idd2gv5e_
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.0 — automated matches

CATH v4.4 (10 domains)

Domain ID domain_id2gv5A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2gv5A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2gv5B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2gv5B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2gv5C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1760
Domain ID domain_id2gv5D01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2gv5D02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2gv5E01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2gv5E02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2gv5F00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1760

8. Citations (1)

9. Files and Curves (10)