8thc

Structure of the Saccharomyces cerevisiae clamp unloader Elg1-RFC bound to a cracked PCNA

Method: ELECTRON MICROSCOPY Dmax: 140.9 Å Quality: GOOD

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

ELG1 isoform 1

Saccharomyces cerevisiae

UniProt A0A8H4F7G7

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–791 Not recorded Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Proliferating cell nuclear antigen × 3 (A0A6B7JGY6) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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.

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

View Construct and Data Evidence
UniProt name A0A8H4F7G7_YEASX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–791; UniProt 1–791

Replication factor C subunit 4

Saccharomyces cerevisiae

UniProt P40339

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–323 Not recorded ELG1 isoform 1 × 1 (A0A8H4F7G7) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Proliferating cell nuclear antigen × 3 (A0A6B7JGY6) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC4_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–323; UniProt 1–323

Replication factor C subunit 3

Saccharomyces cerevisiae

UniProt P38629

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–336 Not recorded ELG1 isoform 1 × 1 (A0A8H4F7G7) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) Proliferating cell nuclear antigen × 3 (A0A6B7JGY6) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC3_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–336; UniProt 1–336

Replication factor C subunit 2

Saccharomyces cerevisiae

UniProt P40348

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 1–353 Not recorded ELG1 isoform 1 × 1 (A0A8H4F7G7) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 5 × 1 (P38251) Proliferating cell nuclear antigen × 3 (A0A6B7JGY6) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC2_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–353; UniProt 1–353

Replication factor C subunit 5

Saccharomyces cerevisiae

UniProt P38251

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–354 Not recorded ELG1 isoform 1 × 1 (A0A8H4F7G7) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Proliferating cell nuclear antigen × 3 (A0A6B7JGY6) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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.

49 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC5_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–354; UniProt 1–354

Proliferating cell nuclear antigen

Saccharomyces cerevisiae

UniProt A0A6B7JGY6

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–258 Chain G; UniProt 1–258 Chain H; UniProt 1–258 Not recorded ELG1 isoform 1 × 1 (A0A8H4F7G7) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.67 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6B7JGY6_YEASX
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 3–260; UniProt 1–258 Author chain G; PDBConstruct 3–260; UniProt 1–258 Author chain H; PDBConstruct 3–260; UniProt 1–258

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 8thc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8thc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8thc
Deposition date deposition_date2023-07-14
Structure title titleStructure of the Saccharomyces cerevisiae clamp unloader Elg1-RFC bound to a cracked PCNA
Keywords keywordsDNA replication, DNA sliding clamp, PCNA clamp, clamp loader/unloader, Elg1-RFC unloader, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.10
Radius of gyration Rg (electron density) rg_electron44.58
Forward intensity I(0) i01206440000.00
Molecular weight molecular_weight291180.0 kDa
Excluded volume excluded_volume366280 ų
Envelope volume envelope_volume519140 ų
Hydration-shell volume shell_volume92945 ų
Envelope diameter envelope_diameter144.5
Shell Rg shell_rg53.06
Envelope Rg envelope_rg43.36
Shape Rg shape_rg44.61
Total Rg total_rg44.84
Total atoms total_atoms20430
Residues n_residues2558
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 dmax140.9
Rg (real space) rg_real44.82
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real1.2060e+09
I(0) uncertainty (real space) i0_real_error1.7010e+07
Rg (reciprocal space) rg_reciprocal45.10
I(0) (reciprocal space) i0_reciprocal1207000000.0000
Solution quality estimate total_estimate0.8972
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.4
Skewness Skewness skewness0.105
Kurtosis Kurtosis kurtosis-0.539
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha162400000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)