5u8s

Structure of eukaryotic CMG helicase at a replication fork

Method: ELECTRON MICROSCOPY Dmax: 191.3 Å Quality: GOOD

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

DNA replication complex GINS protein PSF1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 1–194; UniProt 1–194

DNA replication complex GINS protein SLD5

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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 (strain ATCC 204508 / S288c)

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 × 11 DNA 2 PDB declaration: tridecameric(13) 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) DNA (26-MER) × 1 ;DNA (5'-D(P*AP*TP*CP*GP*AP*TP*CP*GP*AP*TP*CP*GP*AP*T)-3') ; × 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 Å R-free 0.391

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

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 5u8s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5u8s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5u8s
Deposition date deposition_date2016-12-14
Structure title titleStructure of eukaryotic CMG helicase at a replication fork
Keywords keywordsCMG helicase, replisome, origin initiation, DNA polymerase, DNA replication, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.09
Radius of gyration Rg (electron density) rg_electron56.80
Forward intensity I(0) i04890880000.00
Molecular weight molecular_weight584360.0 kDa
Excluded volume excluded_volume730200 ų
Envelope volume envelope_volume1073300 ų
Hydration-shell volume shell_volume150560 ų
Envelope diameter envelope_diameter204.1
Shell Rg shell_rg64.43
Envelope Rg envelope_rg55.64
Shape Rg shape_rg56.82
Total Rg total_rg56.91
Total atoms total_atoms41018
Residues n_residues5101
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 dmax191.3
Rg (real space) rg_real56.90
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real4.8910e+09
I(0) uncertainty (real space) i0_real_error1.0210e+08
Rg (reciprocal space) rg_reciprocal57.24
I(0) (reciprocal space) i0_reciprocal4893000000.0000
Solution quality estimate total_estimate0.8665
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary68.3
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha785100000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.873

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)