8fs8

Structure of S. cerevisiae Rad24-RFC loading the 9-1-1 clamp onto a 5-nt gapped DNA (9-1-1 encircling fully bound DNA)

Method: ELECTRON MICROSCOPY Dmax: 130.8 Å Quality: GOOD

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

Checkpoint protein RAD24

Saccharomyces cerevisiae

UniProt P32641

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 3 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 1–499 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) DNA damage checkpoint control protein MEC3 × 1 (Q02574) DNA damage checkpoint control protein RAD17 × 1 (A0A8H4BW58) DDC1 isoform 1 × 1 (A0A8H4BUG7) Template strand × 1 Primer strand 1 × 1 Primer strand 2 × 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 3.04 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAD24_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–499; UniProt 1–499

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 3 PDB declaration: undecameric(11) Consistent with all polymer counts Chain B; UniProt 1–323 Not recorded Checkpoint protein RAD24 × 1 (P32641) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) DNA damage checkpoint control protein MEC3 × 1 (Q02574) DNA damage checkpoint control protein RAD17 × 1 (A0A8H4BW58) DDC1 isoform 1 × 1 (A0A8H4BUG7) Template strand × 1 Primer strand 1 × 1 Primer strand 2 × 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 3.04 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 3 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 1–336 Not recorded Checkpoint protein RAD24 × 1 (P32641) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 2 × 1 (P40348) Replication factor C subunit 5 × 1 (P38251) DNA damage checkpoint control protein MEC3 × 1 (Q02574) DNA damage checkpoint control protein RAD17 × 1 (A0A8H4BW58) DDC1 isoform 1 × 1 (A0A8H4BUG7) Template strand × 1 Primer strand 1 × 1 Primer strand 2 × 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 3.04 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–DNA Heteromer Protein × 8 DNA 3 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 1–353 Not recorded Checkpoint protein RAD24 × 1 (P32641) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 5 × 1 (P38251) DNA damage checkpoint control protein MEC3 × 1 (Q02574) DNA damage checkpoint control protein RAD17 × 1 (A0A8H4BW58) DDC1 isoform 1 × 1 (A0A8H4BUG7) Template strand × 1 Primer strand 1 × 1 Primer strand 2 × 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 3.04 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 3 PDB declaration: undecameric(11) Consistent with all polymer counts Chain E; UniProt 1–354 Not recorded Checkpoint protein RAD24 × 1 (P32641) Replication factor C subunit 4 × 1 (P40339) Replication factor C subunit 3 × 1 (P38629) Replication factor C subunit 2 × 1 (P40348) DNA damage checkpoint control protein MEC3 × 1 (Q02574) DNA damage checkpoint control protein RAD17 × 1 (A0A8H4BW58) DDC1 isoform 1 × 1 (A0A8H4BUG7) Template strand × 1 Primer strand 1 × 1 Primer strand 2 × 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 3.04 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

DNA damage checkpoint control protein MEC3

Saccharomyces cerevisiae

UniProt Q02574

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 3 PDB declaration: undecameric(11) Consistent with all polymer counts Chain F; UniProt 1–474 Not recorded Checkpoint protein RAD24 × 1 (P32641) 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 damage checkpoint control protein RAD17 × 1 (A0A8H4BW58) DDC1 isoform 1 × 1 (A0A8H4BUG7) Template strand × 1 Primer strand 1 × 1 Primer strand 2 × 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 3.04 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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MEC3_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–474; UniProt 1–474

DNA damage checkpoint control protein RAD17

Saccharomyces cerevisiae

UniProt A0A8H4BW58

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 3 PDB declaration: undecameric(11) Consistent with all polymer counts Chain G; UniProt 1–401 Not recorded Checkpoint protein RAD24 × 1 (P32641) 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 damage checkpoint control protein MEC3 × 1 (Q02574) DDC1 isoform 1 × 1 (A0A8H4BUG7) Template strand × 1 Primer strand 1 × 1 Primer strand 2 × 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 3.04 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8H4BW58_YEASX
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–401; UniProt 1–401

DDC1 isoform 1

Saccharomyces cerevisiae

UniProt A0A8H4BUG7

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 3 PDB declaration: undecameric(11) Consistent with all polymer counts Chain H; UniProt 1–612 Not recorded Checkpoint protein RAD24 × 1 (P32641) 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 damage checkpoint control protein MEC3 × 1 (Q02574) DNA damage checkpoint control protein RAD17 × 1 (A0A8H4BW58) Template strand × 1 Primer strand 1 × 1 Primer strand 2 × 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 3.04 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8H4BUG7_YEASX
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–612; UniProt 1–612

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 8fs8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fs8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8fs8
Deposition date deposition_date2023-01-09
Structure title titleStructure of S. cerevisiae Rad24-RFC loading the 9-1-1 clamp onto a 5-nt gapped DNA (9-1-1 encircling fully bound DNA)
Keywords keywords;DNA damage repair, Rad24-RFC, 9-1-1 clamp, DNA clamp, alternative clamp loader, DNA damage signaling, DNA BINDING PROTEIN-DNA complex, CELL CYCLE-DNA complex ;; CELL CYCLE/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.84
Radius of gyration Rg (electron density) rg_electron42.27
Forward intensity I(0) i01505780000.00
Molecular weight molecular_weight313210.0 kDa
Excluded volume excluded_volume388870 ų
Envelope volume envelope_volume517410 ų
Hydration-shell volume shell_volume95610 ų
Envelope diameter envelope_diameter136.4
Shell Rg shell_rg52.24
Envelope Rg envelope_rg41.44
Shape Rg shape_rg42.29
Total Rg total_rg42.61
Total atoms total_atoms21906
Residues n_residues2637
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 dmax130.8
Rg (real space) rg_real42.54
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.5060e+09
I(0) uncertainty (real space) i0_real_error2.3490e+07
Rg (reciprocal space) rg_reciprocal42.84
I(0) (reciprocal space) i0_reciprocal1506000000.0000
Solution quality estimate total_estimate0.8229
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.6
Skewness Skewness skewness0.047
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha355200000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8fs8E01
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_id8fs8E02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology272 — Zinc Finger, Delta Prime; domain 3
Homologous superfamily homologous superfamily10

8. Citations (2)

9. Files and Curves (10)