6u0m

Structure of the S. cerevisiae replicative helicase CMG in complex with a forked DNA

Method: ELECTRON MICROSCOPY Dmax: 196.0 Å Quality: GOOD

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

DNA replication complex GINS protein PSF1

Saccharomyces cerevisiae

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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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

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 3–200 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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–198; UniProt 3–200

DNA replication complex GINS protein PSF3

Saccharomyces cerevisiae

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 3–193 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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–191; UniProt 3–193

DNA replication complex GINS protein SLD5

Saccharomyces cerevisiae

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 3–293 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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–291; UniProt 3–293

Cell division control protein 45

Saccharomyces cerevisiae

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 5–650 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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1–646; UniProt 5–650

DNA replication licensing factor MCM2

Saccharomyces cerevisiae

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 201–864 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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 6
Chains and sequence ranges Author chain 2; PDBConstruct 1–664; UniProt 201–864

DNA replication licensing factor MCM3

Saccharomyces cerevisiae

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 17–738 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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 7
Chains and sequence ranges Author chain 3; PDBConstruct 1–722; UniProt 17–738

DNA replication licensing factor MCM4

Saccharomyces cerevisiae

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 177–929 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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 8
Chains and sequence ranges Author chain 4; PDBConstruct 1–753; UniProt 177–929

Minichromosome maintenance protein 5

Saccharomyces cerevisiae

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 24–693 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 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 DNA replication licensing factor MCM7 × 1 (P38132) DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 9
Chains and sequence ranges Author chain 5; PDBConstruct 1–670; UniProt 24–693

DNA replication licensing factor MCM7

Saccharomyces cerevisiae

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 1–729 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 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 DNA (26-MER) × 1 DNA (15-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 11
Chains and sequence ranges Author chain 7; PDBConstruct 1–729; UniProt 1–729

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 6u0m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6u0m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6u0m
Deposition date deposition_date2019-08-14
Structure title titleStructure of the S. cerevisiae replicative helicase CMG in complex with a forked DNA
Keywords keywordsDNA replication, CMG-Mcm10, 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_guinier58.58
Radius of gyration Rg (electron density) rg_electron58.36
Forward intensity I(0) i04917200000.00
Molecular weight molecular_weight586060.0 kDa
Excluded volume excluded_volume732390 ų
Envelope volume envelope_volume1167500 ų
Hydration-shell volume shell_volume159450 ų
Envelope diameter envelope_diameter211.2
Shell Rg shell_rg66.32
Envelope Rg envelope_rg56.95
Shape Rg shape_rg58.38
Total Rg total_rg58.46
Total atoms total_atoms41146
Residues n_residues5139
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 dmax196.0
Rg (real space) rg_real58.37
Rg uncertainty (real space) rg_real_error1.39
I(0) (real space) i0_real4.9170e+09
I(0) uncertainty (real space) i0_real_error9.9280e+07
Rg (reciprocal space) rg_reciprocal58.74
I(0) (reciprocal space) i0_reciprocal4920000000.0000
Solution quality estimate total_estimate0.8636
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.6
Skewness Skewness skewness0.275
Kurtosis Kurtosis kurtosis-0.304
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha1113000000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.829

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 7 domains

CATH v4.4 (7 domains)

Domain ID domain_id6u0m201
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1640 — mini-chromosome maintenance (MCM) complex, chain A, domain 1
Homologous superfamily homologous superfamily10 — mini-chromosome maintenance (MCM) complex, chain A, domain 1
Domain ID domain_id6u0m401
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1640 — mini-chromosome maintenance (MCM) complex, chain A, domain 1
Homologous superfamily homologous superfamily10 — mini-chromosome maintenance (MCM) complex, chain A, domain 1
Domain ID domain_id6u0m501
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_id6u0m601
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1640 — mini-chromosome maintenance (MCM) complex, chain A, domain 1
Homologous superfamily homologous superfamily10 — mini-chromosome maintenance (MCM) complex, chain A, domain 1
Domain ID domain_id6u0m602
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_id6u0m701
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_id6u0mC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily2050

8. Citations (1)

9. Files and Curves (10)