5xw5

Crystal structure of budding yeast Cdc14p (C283S) bound to a Swi6p phosphopeptide

Method: X-RAY DIFFRACTION Dmax: 98.8 Å Quality: REASONABLE

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

Tyrosine-protein phosphatase CDC14

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q00684

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–374 Fragment:UNP residues 1-374 Mutation:C283S Regulatory protein SWI6 × 1 (P09959) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;Bis-Tris, ammonium sulfate, PEG 4000 Resolution 1.85 Å R-free 0.217
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–374 Fragment:UNP residues 1-374 Mutation:C283S SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;Bis-Tris, ammonium sulfate, PEG 4000 Resolution 1.85 Å R-free 0.217

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 CDC14_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 42–415; UniProt 1–374 Author chain B; PDBConstruct 42–415; UniProt 1–374

Regulatory protein SWI6

OrganismNot specified

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 155–164 Fragment:UNP residues 155-164 Non-standard monomer:Yes (specific site not provided by mmCIF) Tyrosine-protein phosphatase CDC14 × 1 (Q00684) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;Bis-Tris, ammonium sulfate, PEG 4000 Resolution 1.85 Å R-free 0.217

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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–10; UniProt 155–164

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 5xw5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5xw5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5xw5
Deposition date deposition_date2017-06-29
Structure title titleCrystal structure of budding yeast Cdc14p (C283S) bound to a Swi6p phosphopeptide
Keywords keywordsphosphatase, 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_guinier29.08
Radius of gyration Rg (electron density) rg_electron28.09
Forward intensity I(0) i0106440000.00
Molecular weight molecular_weight83675.0 kDa
Excluded volume excluded_volume105380 ų
Envelope volume envelope_volume125190 ų
Hydration-shell volume shell_volume36757 ų
Envelope diameter envelope_diameter107.4
Shell Rg shell_rg35.90
Envelope Rg envelope_rg28.59
Shape Rg shape_rg28.10
Total Rg total_rg28.80
Total atoms total_atoms5922
Residues n_residues733
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 dmax98.8
Rg (real space) rg_real29.01
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real1.0640e+08
I(0) uncertainty (real space) i0_real_error1.6510e+06
Rg (reciprocal space) rg_reciprocal29.04
I(0) (reciprocal space) i0_reciprocal106400000.0000
Solution quality estimate total_estimate0.6631
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.1
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.425
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33260000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.977; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)