8rif

Cryo-EM structure of the MCM double hexamer loaded onto dsDNA.

Method: ELECTRON MICROSCOPY Dmax: 250.9 Å Quality: GOOD

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

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 2; UniProt 1–868 Chain A; UniProt 1–868 Not recorded DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) DNA (53-MER) × 1 DNA (53-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 1
Chains and sequence ranges Author chain 2; PDBConstruct 1–868; UniProt 1–868 Author chain A; PDBConstruct 1–868; UniProt 1–868

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 3; UniProt 1–971 Chain B; UniProt 1–971 Not recorded DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) DNA (53-MER) × 1 DNA (53-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 2
Chains and sequence ranges Author chain 3; PDBConstruct 36–1006; UniProt 1–971 Author chain B; PDBConstruct 36–1006; UniProt 1–971

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 4; UniProt 1–933 Chain C; UniProt 1–933 Not recorded DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) DNA (53-MER) × 1 DNA (53-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 3
Chains and sequence ranges Author chain 4; PDBConstruct 1–933; UniProt 1–933 Author chain C; PDBConstruct 1–933; UniProt 1–933

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 5; UniProt 1–775 Chain D; UniProt 1–775 Not recorded DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) DNA replication licensing factor MCM6 × 2 (P53091) DNA replication licensing factor MCM7 × 2 (P38132) DNA (53-MER) × 1 DNA (53-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 4
Chains and sequence ranges Author chain 5; PDBConstruct 1–775; UniProt 1–775 Author chain D; PDBConstruct 1–775; UniProt 1–775

DNA replication licensing factor MCM6

Saccharomyces cerevisiae

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 Chain E; UniProt 1–1017 Not recorded DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM7 × 2 (P38132) DNA (53-MER) × 1 DNA (53-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 5
Chains and sequence ranges Author chain 6; PDBConstruct 1–1017; UniProt 1–1017 Author chain E; PDBConstruct 1–1017; UniProt 1–1017

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 × 12 DNA 2 PDB declaration: 14-meric(14) Consistent with all polymer counts Chain 7; UniProt 1–845 Chain F; UniProt 1–845 Not recorded DNA replication licensing factor MCM2 × 2 (P29469) DNA replication licensing factor MCM3 × 2 (P24279) DNA replication licensing factor MCM4 × 2 (P30665) Minichromosome maintenance protein 5 × 2 (P29496) DNA replication licensing factor MCM6 × 2 (P53091) DNA (53-MER) × 1 DNA (53-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 8 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.79 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 6
Chains and sequence ranges Author chain 7; PDBConstruct 1–845; UniProt 1–845 Author chain F; 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 8rif

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8rif
Deposition date deposition_date2023-12-18
Structure title titleCryo-EM structure of the MCM double hexamer loaded onto dsDNA.
Keywords keywordsMCM helicase, DNA replication, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.62
Radius of gyration Rg (electron density) rg_electron71.00
Forward intensity I(0) i012309500000.00
Molecular weight molecular_weight915860.0 kDa
Excluded volume excluded_volume1137100 ų
Envelope volume envelope_volume1785800 ų
Hydration-shell volume shell_volume203860 ų
Envelope diameter envelope_diameter250.0
Shell Rg shell_rg74.85
Envelope Rg envelope_rg69.16
Shape Rg shape_rg71.03
Total Rg total_rg70.98
Total atoms total_atoms64125
Residues n_residues7924
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 dmax250.9
Rg (real space) rg_real73.63
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real1.2310e+10
I(0) uncertainty (real space) i0_real_error2.5610e+08
Rg (reciprocal space) rg_reciprocal70.40
I(0) (reciprocal space) i0_reciprocal12300000000.0000
Solution quality estimate total_estimate0.8817
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.8
Skewness Skewness skewness0.514
Kurtosis Kurtosis kurtosis-0.192
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha1.1950
Highest regularization parameter α highest_alpha5997000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.745; Stabil: 0.884; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.620

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)