9uq0

Structure of human MCM2-7 single hexamer with MCM3-WHD attached to MCM2-CTD

Method: ELECTRON MICROSCOPY Dmax: 164.5 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ZN ZINC ION × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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 1–808 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ZN ZINC ION × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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 1–808; UniProt 1–808

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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ZN ZINC ION × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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 1–863; 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ZN ZINC ION × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ZN ZINC ION × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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) ATP ADENOSINE-5'-TRIPHOSPHATE × 3 ZN ZINC ION × 4 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.47 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 9uq0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9uq0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9uq0
Deposition date deposition_date2025-04-29
Structure title titleStructure of human MCM2-7 single hexamer with MCM3-WHD attached to MCM2-CTD
Keywords keywordsHelicase, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.47
Radius of gyration Rg (electron density) rg_electron51.03
Forward intensity I(0) i02466220000.00
Molecular weight molecular_weight407190.0 kDa
Excluded volume excluded_volume506460 ų
Envelope volume envelope_volume756930 ų
Hydration-shell volume shell_volume118760 ų
Envelope diameter envelope_diameter172.3
Shell Rg shell_rg58.70
Envelope Rg envelope_rg49.76
Shape Rg shape_rg51.08
Total Rg total_rg51.08
Total atoms total_atoms28580
Residues n_residues3756
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 dmax164.5
Rg (real space) rg_real51.25
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real2.4660e+09
I(0) uncertainty (real space) i0_real_error5.0750e+07
Rg (reciprocal space) rg_reciprocal51.64
I(0) (reciprocal space) i0_reciprocal2468000000.0000
Solution quality estimate total_estimate0.8790
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.7
Skewness Skewness skewness0.152
Kurtosis Kurtosis kurtosis-0.387
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha289000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.835

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)