9e2y

Cryo-EM structure of yeast CMG helicase stalled at G4-containing DNA template, state 3

Method: ELECTRON MICROSCOPY Dmax: 191.7 Å Quality: GOOD

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

DNA replication complex GINS protein PSF1

Saccharomyces cerevisiae W303

UniProt Q12488

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain A; UniProt 1–208 Not recorded DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSF1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–208; UniProt 1–208

DNA replication complex GINS protein PSF2

Saccharomyces cerevisiae W303

UniProt P40359

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain B; UniProt 1–213 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSF2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–213; UniProt 1–213

DNA replication complex GINS protein PSF3

Saccharomyces cerevisiae W303

UniProt Q12146

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain C; UniProt 1–194 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSF3_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 24–217; UniProt 1–194

DNA replication complex GINS protein SLD5

Saccharomyces cerevisiae W303

UniProt Q03406

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain D; UniProt 1–294 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SLD5_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–294; UniProt 1–294

Cell division control protein 45

Saccharomyces cerevisiae W303

UniProt Q08032

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain E; UniProt 1–650 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

34 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC45_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–650; UniProt 1–650

DNA replication licensing factor MCM2

Saccharomyces cerevisiae W303

UniProt P29469

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 2; UniProt 1–868 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

51 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM2_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain 2; PDBConstruct 1–868; UniProt 1–868

DNA replication licensing factor MCM3

Saccharomyces cerevisiae W303

UniProt P24279

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 3; UniProt 1–971 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

59 other PDB entries and 59 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM3_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain 3; PDBConstruct 1–971; UniProt 1–971

DNA replication licensing factor MCM4

Saccharomyces cerevisiae W303

UniProt P30665

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 4; UniProt 1–933 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

58 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM4_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain 4; PDBConstruct 1–933; UniProt 1–933

Minichromosome maintenance protein 5

Saccharomyces cerevisiae W303

UniProt P29496

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 5; UniProt 1–775 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

54 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM5_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain 5; PDBConstruct 1–775; UniProt 1–775

DNA replication licensing factor MCM6

Saccharomyces cerevisiae W303

UniProt P53091

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 6; UniProt 1–1017 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM7 × 1 (P38132) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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.

58 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM6_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain 6; PDBConstruct 1–1017; UniProt 1–1017

DNA replication licensing factor MCM7

Saccharomyces cerevisiae W303

UniProt P38132

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 7; UniProt 1–845 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) Topoisomerase 1-associated factor 1 × 1 (P53840) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM7_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain 7; PDBConstruct 1–845; UniProt 1–845

Topoisomerase 1-associated factor 1

Saccharomyces cerevisiae W303

UniProt P53840

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain X; UniProt 354–396 Not recorded DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) Leading strand DNA template × 1 Lagging strand DNA template × 1 DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 6 ZN ZINC ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;Wait time 30 seconds after sample application; blot time 30 seconds with blot force 0 Resolution 3.20 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 TOF1_YEAST
Isoform
PDB entities 14
Chains and sequence ranges Author chain X; PDBConstruct 1–43; UniProt 354–396

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 9e2y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e2y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e2y
Deposition date deposition_date2024-10-23
最后修订 last_revision2025-03-26
Structure title titleCryo-EM structure of yeast CMG helicase stalled at G4-containing DNA template, state 3
Keywords keywordshelicase, DNA replication, cell division, fork stalling, translocation, REPLICATION, REPLICATION-DNA complex; REPLICATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.19
Radius of gyration Rg (electron density) rg_electron57.17
Forward intensity I(0) i05132950000.00
Molecular weight molecular_weight597050.0 kDa
Excluded volume excluded_volume745150 ų
Envelope volume envelope_volume1091500 ų
Hydration-shell volume shell_volume151620 ų
Envelope diameter envelope_diameter203.4
Shell Rg shell_rg64.92
Envelope Rg envelope_rg56.27
Shape Rg shape_rg57.19
Total Rg total_rg57.23
Total atoms total_atoms83461
Residues n_residues5170
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 dmax191.7
Rg (real space) rg_real57.01
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real5.1330e+09
I(0) uncertainty (real space) i0_real_error1.0070e+08
Rg (reciprocal space) rg_reciprocal57.32
I(0) (reciprocal space) i0_reciprocal5135000000.0000
Solution quality estimate total_estimate0.8615
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary71.0
Skewness Skewness skewness0.291
Kurtosis Kurtosis kurtosis-0.291
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha784000000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.813

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

8. Citations (1)

9. Files and Curves (10)