4c93

Crystal structure of the carboxy-terminal domain of yeast Ctf4 bound to Pol alpha.

Method: X-RAY DIFFRACTION Dmax: 109.3 Å Quality: EXCELLENT

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

DNA POLYMERASE ALPHA-BINDING PROTEIN

SACCHAROMYCES CEREVISIAE

UniProt Q01454

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 471–927 Chain B; UniProt 471–927 Chain C; UniProt 471–927 Fragment:C-TERMINAL DOMAIN, RESIDUES 471-927 DNA POLYMERASE ALPHA CATALYTIC SUBUNIT A × 2 (P13382) X-RAY DIFFRACTION X-ray crystallization conditions:0.2 M TRI-SODIUM CITRATE PH 6.2, 7-9% PEG 8000 Resolution 2.69 Å R-free 0.210

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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTF4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–478; UniProt 471–927 Author chain B; PDBConstruct 22–478; UniProt 471–927 Author chain C; PDBConstruct 22–478; UniProt 471–927

DNA POLYMERASE ALPHA CATALYTIC SUBUNIT A

OrganismNot specified

UniProt P13382

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 137–149 Chain E; UniProt 137–149 Fragment:CTF4-BINDING MOTIF, RESIDUES 137-149 DNA POLYMERASE ALPHA-BINDING PROTEIN × 3 (Q01454) X-RAY DIFFRACTION X-ray crystallization conditions:0.2 M TRI-SODIUM CITRATE PH 6.2, 7-9% PEG 8000 Resolution 2.69 Å R-free 0.210

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOA_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–13; UniProt 137–149 Author chain E; PDBConstruct 1–13; UniProt 137–149

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 4c93

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4c93
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4c93
Deposition date deposition_date2013-10-02
Structure title titleCrystal structure of the carboxy-terminal domain of yeast Ctf4 bound to Pol alpha.
Keywords keywordsDNA REPLICATION, ADAPTOR PROTEIN, BETA PROPELLER DOMAIN; DNA REPLICATION
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.67
Radius of gyration Rg (electron density) rg_electron33.71
Forward intensity I(0) i0261228000.00
Molecular weight molecular_weight133590.0 kDa
Excluded volume excluded_volume168390 ų
Envelope volume envelope_volume216440 ų
Hydration-shell volume shell_volume51762 ų
Envelope diameter envelope_diameter112.2
Shell Rg shell_rg41.81
Envelope Rg envelope_rg33.72
Shape Rg shape_rg33.71
Total Rg total_rg34.32
Total atoms total_atoms9433
Residues n_residues1171
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 dmax109.3
Rg (real space) rg_real34.55
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real2.6120e+08
I(0) uncertainty (real space) i0_real_error4.1630e+06
Rg (reciprocal space) rg_reciprocal34.63
I(0) (reciprocal space) i0_reciprocal261200000.0000
Solution quality estimate total_estimate0.9021
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.4
Skewness Skewness skewness0.184
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha84620000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.916

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)