2xfv

Structure of the amino-terminal domain from the cell-cycle regulator Swi6

Method: X-RAY DIFFRACTION Dmax: 66.8 Å Quality: GOOD

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

REGULATORY PROTEIN SWI6

SACCHAROMYCES CEREVISIAE

UniProt P09959

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–126 Chain B; UniProt 2–126 Fragment:AMINO-TERMINAL DOMAIN, RESIDUES 2-126 CA CALCIUM ION × 3 GOL GLYCEROL × 3 ACT ACETATE ION × 1 CAC CACODYLATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;5-15MG/ML PROTEIN, 10% PEG4000, 0.1M NA-CACODYLATE, 20MM CA-ACETATE, 0.2M NH4CL, PH 6.5 Resolution 1.90 Å R-free 0.196

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SWI6_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–125; UniProt 2–126 Author chain B; PDBConstruct 1–125; UniProt 2–126

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 2xfv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2xfv
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2xfv
Deposition date deposition_date2010-05-27
Structure title titleStructure of the amino-terminal domain from the cell-cycle regulator Swi6
Keywords keywordsCELL-CYCLE, REGULATION, 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_guinier21.00
Radius of gyration Rg (electron density) rg_electron19.64
Forward intensity I(0) i011699900.00
Molecular weight molecular_weight25640.0 kDa
Excluded volume excluded_volume32018 ų
Envelope volume envelope_volume38999 ų
Hydration-shell volume shell_volume17198 ų
Envelope diameter envelope_diameter68.8
Shell Rg shell_rg25.13
Envelope Rg envelope_rg19.78
Shape Rg shape_rg19.62
Total Rg total_rg20.51
Total atoms total_atoms1804
Residues n_residues216
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 dmax66.8
Rg (real space) rg_real20.98
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real1.1700e+07
I(0) uncertainty (real space) i0_real_error1.4820e+05
Rg (reciprocal space) rg_reciprocal20.98
I(0) (reciprocal space) i0_reciprocal11700000.0000
Solution quality estimate total_estimate0.8187
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.472
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1985000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2xfvA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology260 — Mlu1-box Binding Protein; DNA-binding Domain
Homologous superfamily homologous superfamily30
Domain ID domain_id2xfvB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology260 — Mlu1-box Binding Protein; DNA-binding Domain
Homologous superfamily homologous superfamily30

8. Citations (1)

9. Files and Curves (10)