9per

Structure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy

Method: ELECTRON MICROSCOPY Dmax: 109.4 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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count 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) ACT ACETATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count 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) ACT ACETATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count 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) ACT ACETATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count 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) ACT ACETATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 4–353 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 2 × 1 (P40348) ACT ACETATE ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.57 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 4–353; UniProt 4–353

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 9per

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9per
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9per
Deposition date deposition_date2025-07-02
Structure title titleStructure of the S. cerevisiae clamp loader Replication Factor C (RFC) with mixed nucleotide occupancy
Keywords keywordsAAA+ ATPase, Rossmann Fold, Complex, DNA replication, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.19
Radius of gyration Rg (electron density) rg_electron35.33
Forward intensity I(0) i0459909000.00
Molecular weight molecular_weight175490.0 kDa
Excluded volume excluded_volume220910 ų
Envelope volume envelope_volume287240 ų
Hydration-shell volume shell_volume64616 ų
Envelope diameter envelope_diameter117.9
Shell Rg shell_rg44.04
Envelope Rg envelope_rg34.82
Shape Rg shape_rg35.34
Total Rg total_rg35.88
Total atoms total_atoms12323
Residues n_residues1550
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 dmax109.4
Rg (real space) rg_real35.95
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real4.5990e+08
I(0) uncertainty (real space) i0_real_error6.7460e+06
Rg (reciprocal space) rg_reciprocal36.10
I(0) (reciprocal space) i0_reciprocal460000000.0000
Solution quality estimate total_estimate0.8983
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.2
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.496
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha106800000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.901

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)