6s2f

Cryo-EM structure of Ctf18-1-8 in complex with the catalytic domain of DNA polymerase epsilon (Class 2)

Method: ELECTRON MICROSCOPY Dmax: 131.5 Å Quality: GOOD

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

DNA polymerase epsilon catalytic subunit A

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P21951

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1192 Not recorded Chromosome transmission fidelity protein 8 × 1 (P38877) Chromosome transmission fidelity protein 18 × 1 (P49956) Sister chromatid cohesion protein DCC1 × 1 (P25559) SF4 IRON/SULFUR CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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.

33 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOE_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 28–1219; UniProt 1–1192

Chromosome transmission fidelity protein 8

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P38877

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–133 Not recorded DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 18 × 1 (P49956) Sister chromatid cohesion protein DCC1 × 1 (P25559) SF4 IRON/SULFUR CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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.

7 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTF8_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–133; UniProt 1–133

Chromosome transmission fidelity protein 18

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P49956

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 713–741 Not recorded DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Sister chromatid cohesion protein DCC1 × 1 (P25559) SF4 IRON/SULFUR CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTF18_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 5–33; UniProt 713–741

Sister chromatid cohesion protein DCC1

Saccharomyces cerevisiae (strain ATCC 204508 / 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–380 Not recorded DNA polymerase epsilon catalytic subunit A × 1 (P21951) Chromosome transmission fidelity protein 8 × 1 (P38877) Chromosome transmission fidelity protein 18 × 1 (P49956) SF4 IRON/SULFUR CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.80 Å

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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCC1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–380; UniProt 1–380

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 6s2f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6s2f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6s2f
Deposition date deposition_date2019-06-20
Structure title titleCryo-EM structure of Ctf18-1-8 in complex with the catalytic domain of DNA polymerase epsilon (Class 2)
Keywords keywordsDNA polymerase, PCNA loader, protein complex, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.38
Radius of gyration Rg (electron density) rg_electron40.80
Forward intensity I(0) i0448982000.00
Molecular weight molecular_weight177120.0 kDa
Excluded volume excluded_volume223260 ų
Envelope volume envelope_volume314340 ų
Hydration-shell volume shell_volume64350 ų
Envelope diameter envelope_diameter135.3
Shell Rg shell_rg46.67
Envelope Rg envelope_rg39.80
Shape Rg shape_rg40.78
Total Rg total_rg41.21
Total atoms total_atoms12459
Residues n_residues1539
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 dmax131.5
Rg (real space) rg_real41.28
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real4.4900e+08
I(0) uncertainty (real space) i0_real_error7.3960e+06
Rg (reciprocal space) rg_reciprocal41.38
I(0) (reciprocal space) i0_reciprocal449000000.0000
Solution quality estimate total_estimate0.8914
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.9
Skewness Skewness skewness0.219
Kurtosis Kurtosis kurtosis-0.463
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42300000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.795

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)