7w8g

Cryo-EM structure of MCM double hexamer

Method: ELECTRON MICROSCOPY Dmax: 233.4 Å Quality: GOOD

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

DNA replication licensing factor MCM2

OrganismNot specified

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 heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain 2; UniProt 1–868 Chain B; 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) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 10 MG MAGNESIUM ION × 12 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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 B; PDBConstruct 1–868; UniProt 1–868

DNA replication licensing factor MCM3

OrganismNot specified

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 heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain 3; UniProt 1–971 Chain C; 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) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 10 MG MAGNESIUM ION × 12 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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 1–971; UniProt 1–971 Author chain C; PDBConstruct 1–971; UniProt 1–971

DNA replication licensing factor MCM4

OrganismNot specified

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 heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain 4; UniProt 1–933 Chain D; 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) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 10 MG MAGNESIUM ION × 12 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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 D; PDBConstruct 1–933; UniProt 1–933

Minichromosome maintenance protein 5

OrganismNot specified

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 heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain 5; UniProt 1–775 Chain E; 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) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 10 MG MAGNESIUM ION × 12 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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 E; PDBConstruct 1–775; UniProt 1–775

DNA replication licensing factor MCM6

OrganismNot specified

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 heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain 6; UniProt 1–1017 Chain F; 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) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 10 MG MAGNESIUM ION × 12 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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 F; PDBConstruct 1–1017; UniProt 1–1017

DNA replication licensing factor MCM7

OrganismNot specified

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 heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain 7; UniProt 1–845 Chain G; 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) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 10 MG MAGNESIUM ION × 12 ZN ZINC ION × 10 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.52 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 G; 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 7w8g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7w8g
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7w8g
Deposition date deposition_date2021-12-07
Structure title titleCryo-EM structure of MCM double hexamer
Keywords keywordsDNA replication initiation, Complex, Replicative helicase, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier69.08
Radius of gyration Rg (electron density) rg_electron68.88
Forward intensity I(0) i011242000000.00
Molecular weight molecular_weight890790.0 kDa
Excluded volume excluded_volume1112800 ų
Envelope volume envelope_volume1635300 ų
Hydration-shell volume shell_volume192900 ų
Envelope diameter envelope_diameter215.9
Shell Rg shell_rg72.98
Envelope Rg envelope_rg66.61
Shape Rg shape_rg68.88
Total Rg total_rg68.92
Total atoms total_atoms62460
Residues n_residues7876
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 dmax233.4
Rg (real space) rg_real69.04
Rg uncertainty (real space) rg_real_error1.76
I(0) (real space) i0_real1.1240e+10
I(0) uncertainty (real space) i0_real_error2.2740e+08
Rg (reciprocal space) rg_reciprocal69.13
I(0) (reciprocal space) i0_reciprocal11240000000.0000
Solution quality estimate total_estimate0.8003
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary81.2
Skewness Skewness skewness0.310
Kurtosis Kurtosis kurtosis-0.533
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0010
Highest regularization parameter α highest_alpha1810000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)