8dr1

Consensus closed state of RFC:PCNA bound to a 3' ss/dsDNA junction (DNA2)

Method: ELECTRON MICROSCOPY Dmax: 134.3 Å Quality: GOOD

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

Replication factor C subunit 1

Saccharomyces cerevisiae

UniProt P38630

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–DNA Heteromer Protein × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain A; UniProt 1–861 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 (P15873) ;DNA (5'-D(P*TP*TP*TP*CP*GP*GP*GP*GP*GP*GP*GP*CP*CP*GP*GP*GP*GP*GP*G)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*GP*GP*CP*CP*CP*CP*CP*CP*CP*GP*GP*C)-3') ; × 1 ;DNA (5'-D(P*TP*TP*AP*GP*GP*GP*GP*GP*GP*GP*GP*GP*A)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*TP*TP*T)-3') ; × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.14 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.

30 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFC1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–861; UniProt 1–861

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–DNA Heteromer Protein × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain B; UniProt 1–323 Not recorded Replication factor C subunit 1 × 1 (P38630) 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 (P15873) ;DNA (5'-D(P*TP*TP*TP*CP*GP*GP*GP*GP*GP*GP*GP*CP*CP*GP*GP*GP*GP*GP*G)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*GP*GP*CP*CP*CP*CP*CP*CP*CP*GP*GP*C)-3') ; × 1 ;DNA (5'-D(P*TP*TP*AP*GP*GP*GP*GP*GP*GP*GP*GP*GP*A)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*TP*TP*T)-3') ; × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.14 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–DNA Heteromer Protein × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain C; UniProt 1–340 Not recorded Replication factor C subunit 1 × 1 (P38630) 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 (P15873) ;DNA (5'-D(P*TP*TP*TP*CP*GP*GP*GP*GP*GP*GP*GP*CP*CP*GP*GP*GP*GP*GP*G)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*GP*GP*CP*CP*CP*CP*CP*CP*CP*GP*GP*C)-3') ; × 1 ;DNA (5'-D(P*TP*TP*AP*GP*GP*GP*GP*GP*GP*GP*GP*GP*A)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*TP*TP*T)-3') ; × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.14 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 1–340; UniProt 1–340

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–DNA Heteromer Protein × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain D; UniProt 1–353 Not recorded Replication factor C subunit 1 × 1 (P38630) 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 (P15873) ;DNA (5'-D(P*TP*TP*TP*CP*GP*GP*GP*GP*GP*GP*GP*CP*CP*GP*GP*GP*GP*GP*G)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*GP*GP*CP*CP*CP*CP*CP*CP*CP*GP*GP*C)-3') ; × 1 ;DNA (5'-D(P*TP*TP*AP*GP*GP*GP*GP*GP*GP*GP*GP*GP*A)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*TP*TP*T)-3') ; × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.14 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–DNA Heteromer Protein × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain E; UniProt 1–354 Not recorded Replication factor C subunit 1 × 1 (P38630) 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 (P15873) ;DNA (5'-D(P*TP*TP*TP*CP*GP*GP*GP*GP*GP*GP*GP*CP*CP*GP*GP*GP*GP*GP*G)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*GP*GP*CP*CP*CP*CP*CP*CP*CP*GP*GP*C)-3') ; × 1 ;DNA (5'-D(P*TP*TP*AP*GP*GP*GP*GP*GP*GP*GP*GP*GP*A)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*TP*TP*T)-3') ; × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.14 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 P15873

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–DNA Heteromer Protein × 8 DNA 4 PDB declaration: dodecameric(12) Consistent with all polymer counts Chain F; UniProt 1–258 Chain G; UniProt 1–258 Chain H; UniProt 1–258 Not recorded Replication factor C subunit 1 × 1 (P38630) 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) ;DNA (5'-D(P*TP*TP*TP*CP*GP*GP*GP*GP*GP*GP*GP*CP*CP*GP*GP*GP*GP*GP*G)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*GP*GP*CP*CP*CP*CP*CP*CP*CP*GP*GP*C)-3') ; × 1 ;DNA (5'-D(P*TP*TP*AP*GP*GP*GP*GP*GP*GP*GP*GP*GP*A)-3') ; × 1 ;DNA (5'-D(P*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*TP*TP*T)-3') ; × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.14 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.

55 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCNA_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 20–277; UniProt 1–258 Author chain G; PDBConstruct 20–277; UniProt 1–258 Author chain H; PDBConstruct 20–277; 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 8dr1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8dr1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8dr1
Deposition date deposition_date2022-07-20
Structure title titleConsensus closed state of RFC:PCNA bound to a 3' ss/dsDNA junction (DNA2)
Keywords keywordsREPLICATION-DNA complex; REPLICATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.47
Radius of gyration Rg (electron density) rg_electron43.00
Forward intensity I(0) i01539560000.00
Molecular weight molecular_weight314570.0 kDa
Excluded volume excluded_volume389540 ų
Envelope volume envelope_volume528800 ų
Hydration-shell volume shell_volume96135 ų
Envelope diameter envelope_diameter135.6
Shell Rg shell_rg52.89
Envelope Rg envelope_rg42.12
Shape Rg shape_rg43.03
Total Rg total_rg43.30
Total atoms total_atoms43685
Residues n_residues2671
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 dmax134.3
Rg (real space) rg_real43.17
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.5400e+09
I(0) uncertainty (real space) i0_real_error2.3910e+07
Rg (reciprocal space) rg_reciprocal43.47
I(0) (reciprocal space) i0_reciprocal1540000000.0000
Solution quality estimate total_estimate0.8217
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.9
Skewness Skewness skewness0.068
Kurtosis Kurtosis kurtosis-0.543
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha280200000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8dr1E01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id8dr1E02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily60
Domain ID domain_id8dr1E03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology272 — Zinc Finger, Delta Prime; domain 3
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)