7p30

3.0 A resolution structure of a DNA-loaded MCM double hexamer

Method: ELECTRON MICROSCOPY Dmax: 247.8 Å Quality: GOOD

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

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 × 12 DNA 2 PDB declaration: tetradecameric(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 × 10 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 seconds before plunging Resolution 3.00 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 (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 × 12 DNA 2 PDB declaration: tetradecameric(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 × 10 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 seconds before plunging Resolution 3.00 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 (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 × 12 DNA 2 PDB declaration: tetradecameric(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 × 10 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 seconds before plunging Resolution 3.00 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 (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 × 12 DNA 2 PDB declaration: tetradecameric(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 × 10 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 seconds before plunging Resolution 3.00 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 (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 × 12 DNA 2 PDB declaration: tetradecameric(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 × 10 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 seconds before plunging Resolution 3.00 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 (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 × 12 DNA 2 PDB declaration: tetradecameric(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 × 10 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blotted for 3 seconds before plunging Resolution 3.00 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 7p30

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7p30
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7p30
Deposition date deposition_date2021-07-06
Structure title title3.0 A resolution structure of a DNA-loaded MCM double hexamer
Keywords keywordsMcm2-7 helicase, nucleoprotein complex, AAA+ ATPase, DNA replication, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier69.73
Radius of gyration Rg (electron density) rg_electron70.00
Forward intensity I(0) i011886800000.00
Molecular weight molecular_weight896430.0 kDa
Excluded volume excluded_volume1111500 ų
Envelope volume envelope_volume1719900 ų
Hydration-shell volume shell_volume199260 ų
Envelope diameter envelope_diameter221.4
Shell Rg shell_rg74.02
Envelope Rg envelope_rg67.88
Shape Rg shape_rg70.02
Total Rg total_rg69.98
Total atoms total_atoms123819
Residues n_residues7750
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 dmax247.8
Rg (real space) rg_real72.74
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real1.1890e+10
I(0) uncertainty (real space) i0_real_error2.3820e+08
Rg (reciprocal space) rg_reciprocal69.61
I(0) (reciprocal space) i0_reciprocal11880000000.0000
Solution quality estimate total_estimate0.8894
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary78.8
Skewness Skewness skewness0.502
Kurtosis Kurtosis kurtosis-0.194
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha1.1890
Highest regularization parameter α highest_alpha5172000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 0.885; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.690

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)