5msn

Structure of the Dcc1 Protein

Method: X-RAY DIFFRACTION Dmax: 113.7 Å Quality: EXCELLENT

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

DCC1 protein

Saccharomyces cerevisiae S288c

UniProt P25559

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 90–380 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2M potassium sodium tartrate and 18% PEG 3,350 Resolution 2.00 Å R-free 0.230
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 90–380 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2M potassium sodium tartrate and 18% PEG 3,350 Resolution 2.00 Å R-free 0.230
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 90–380 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2M potassium sodium tartrate and 18% PEG 3,350 Resolution 2.00 Å R-free 0.230
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 90–380 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2M potassium sodium tartrate and 18% PEG 3,350 Resolution 2.00 Å R-free 0.230

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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCC1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–293; UniProt 90–380 Author chain B; PDBConstruct 3–293; UniProt 90–380 Author chain C; PDBConstruct 3–293; UniProt 90–380 Author chain D; PDBConstruct 3–293; UniProt 90–380

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 5msn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5msn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5msn
Deposition date deposition_date2017-01-05
Structure title titleStructure of the Dcc1 Protein
Keywords keywordswinged-helix, DNA repair, 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_guinier35.77
Radius of gyration Rg (electron density) rg_electron34.99
Forward intensity I(0) i0199392000.00
Molecular weight molecular_weight118560.0 kDa
Excluded volume excluded_volume150530 ų
Envelope volume envelope_volume200200 ų
Hydration-shell volume shell_volume47340 ų
Envelope diameter envelope_diameter112.1
Shell Rg shell_rg41.96
Envelope Rg envelope_rg34.42
Shape Rg shape_rg34.98
Total Rg total_rg35.53
Total atoms total_atoms8358
Residues n_residues1025
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 dmax113.7
Rg (real space) rg_real35.71
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real1.9940e+08
I(0) uncertainty (real space) i0_real_error3.6570e+06
Rg (reciprocal space) rg_reciprocal35.75
I(0) (reciprocal space) i0_reciprocal199400000.0000
Solution quality estimate total_estimate0.9049
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.8
Skewness Skewness skewness0.247
Kurtosis Kurtosis kurtosis-0.615
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33510000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.954

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)