7tfj

Atomic model of S. cerevisiae clamp-clamp loader complex PCNA-RFC bound to DNA with a closed clamp ring

Method: ELECTRON MICROSCOPY Dmax: 127.6 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 2 PDB declaration: decameric(10) 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) Template strand × 1 Primer strand × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2 PDB declaration: decameric(10) 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) Template strand × 1 Primer strand × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2 PDB declaration: decameric(10) 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) Template strand × 1 Primer strand × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2 PDB declaration: decameric(10) 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) Template strand × 1 Primer strand × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2 PDB declaration: decameric(10) 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) Template strand × 1 Primer strand × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain F; UniProt 1–258 Chain G; UniProt 1–258 Chain H; UniProt 1–258 Non-standard monomer:Yes (specific site not provided by mmCIF) 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) Template strand × 1 Primer strand × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 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 7tfj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7tfj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7tfj
Deposition date deposition_date2022-01-06
Structure title titleAtomic model of S. cerevisiae clamp-clamp loader complex PCNA-RFC bound to DNA with a closed clamp ring
Keywords keywordsDNA replication, DNA damage repair, RFC loader, PCNA clamp, DNA polymerase processivity factor, DNA binding protein-DNA complex; DNA BINDING PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.61
Radius of gyration Rg (electron density) rg_electron42.28
Forward intensity I(0) i01343540000.00
Molecular weight molecular_weight295440.0 kDa
Excluded volume excluded_volume366590 ų
Envelope volume envelope_volume497620 ų
Hydration-shell volume shell_volume92367 ų
Envelope diameter envelope_diameter133.3
Shell Rg shell_rg51.79
Envelope Rg envelope_rg41.48
Shape Rg shape_rg42.29
Total Rg total_rg42.62
Total atoms total_atoms20607
Residues n_residues2510
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 dmax127.6
Rg (real space) rg_real42.36
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real1.3440e+09
I(0) uncertainty (real space) i0_real_error2.1110e+07
Rg (reciprocal space) rg_reciprocal42.61
I(0) (reciprocal space) i0_reciprocal1344000000.0000
Solution quality estimate total_estimate0.8857
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.7
Skewness Skewness skewness0.117
Kurtosis Kurtosis kurtosis-0.525
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha279100000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.701

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7tfjE01
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_id7tfjE02
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)