8w0i

Cryo-EM structure of the human MCM2-7 heterohexamer

Method: ELECTRON MICROSCOPY Dmax: 152.4 Å Quality: GOOD

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

DNA replication licensing factor MCM2

Homo sapiens

UniProt P49736

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 2; UniProt 1–904 Not recorded DNA replication licensing factor MCM3 × 1 (P25205) DNA replication licensing factor MCM4 × 1 (P33991) DNA replication licensing factor MCM5 × 1 (P33992) DNA replication licensing factor MCM6 × 1 (Q14566) DNA replication licensing factor MCM7 × 1 (P33993) ZN ZINC ION × 5 MG MAGNESIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

38 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain 2; PDBConstruct 1–904; UniProt 1–904

DNA replication licensing factor MCM3

Homo sapiens

UniProt P25205

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 3; UniProt 2–808 Not recorded DNA replication licensing factor MCM2 × 1 (P49736) DNA replication licensing factor MCM4 × 1 (P33991) DNA replication licensing factor MCM5 × 1 (P33992) DNA replication licensing factor MCM6 × 1 (Q14566) DNA replication licensing factor MCM7 × 1 (P33993) ZN ZINC ION × 5 MG MAGNESIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 MCM3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain 3; PDBConstruct 4–810; UniProt 2–808

DNA replication licensing factor MCM4

Homo sapiens

UniProt P33991

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 4; UniProt 1–863 Not recorded DNA replication licensing factor MCM2 × 1 (P49736) DNA replication licensing factor MCM3 × 1 (P25205) DNA replication licensing factor MCM5 × 1 (P33992) DNA replication licensing factor MCM6 × 1 (Q14566) DNA replication licensing factor MCM7 × 1 (P33993) ZN ZINC ION × 5 MG MAGNESIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 MCM4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain 4; PDBConstruct 4–866; UniProt 1–863

DNA replication licensing factor MCM5

Homo sapiens

UniProt P33992

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 5; UniProt 1–734 Not recorded DNA replication licensing factor MCM2 × 1 (P49736) DNA replication licensing factor MCM3 × 1 (P25205) DNA replication licensing factor MCM4 × 1 (P33991) DNA replication licensing factor MCM6 × 1 (Q14566) DNA replication licensing factor MCM7 × 1 (P33993) ZN ZINC ION × 5 MG MAGNESIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MCM5_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain 5; PDBConstruct 1–734; UniProt 1–734

DNA replication licensing factor MCM6

Homo sapiens

UniProt Q14566

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 6; UniProt 1–821 Not recorded DNA replication licensing factor MCM2 × 1 (P49736) DNA replication licensing factor MCM3 × 1 (P25205) DNA replication licensing factor MCM4 × 1 (P33991) DNA replication licensing factor MCM5 × 1 (P33992) DNA replication licensing factor MCM7 × 1 (P33993) ZN ZINC ION × 5 MG MAGNESIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 MCM6_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain 6; PDBConstruct 1–821; UniProt 1–821

DNA replication licensing factor MCM7

Homo sapiens

UniProt P33993

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain 7; UniProt 1–719 Not recorded DNA replication licensing factor MCM2 × 1 (P49736) DNA replication licensing factor MCM3 × 1 (P25205) DNA replication licensing factor MCM4 × 1 (P33991) DNA replication licensing factor MCM5 × 1 (P33992) DNA replication licensing factor MCM6 × 1 (Q14566) ZN ZINC ION × 5 MG MAGNESIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 MCM7_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain 7; PDBConstruct 1–719; UniProt 1–719

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 8w0i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8w0i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8w0i
Deposition date deposition_date2024-02-13
Structure title titleCryo-EM structure of the human MCM2-7 heterohexamer
Keywords keywordscomplex, helicase, replication, AAA+ ATPase, DNA BINDING PROTEIN; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.39
Radius of gyration Rg (electron density) rg_electron49.87
Forward intensity I(0) i02412820000.00
Molecular weight molecular_weight405210.0 kDa
Excluded volume excluded_volume505640 ų
Envelope volume envelope_volume733750 ų
Hydration-shell volume shell_volume117120 ų
Envelope diameter envelope_diameter161.3
Shell Rg shell_rg58.25
Envelope Rg envelope_rg48.44
Shape Rg shape_rg49.90
Total Rg total_rg50.01
Total atoms total_atoms56930
Residues n_residues3557
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 dmax152.4
Rg (real space) rg_real50.15
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real2.4130e+09
I(0) uncertainty (real space) i0_real_error4.2770e+07
Rg (reciprocal space) rg_reciprocal50.59
I(0) (reciprocal space) i0_reciprocal2414000000.0000
Solution quality estimate total_estimate0.8704
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.8
Skewness Skewness skewness0.078
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha283000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.561

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)