9lxf

Structure of extended DNA-free MCM DH at 3.8 Angstroms resolution

Method: ELECTRON MICROSCOPY Dmax: 222.3 Å Quality: GOOD

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

DNA replication licensing factor MCM2

OrganismNot specified

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain 2; UniProt 1–904 Chain D; UniProt 1–904 Not recorded Isoform 2 of DNA replication licensing factor MCM3 × 4 (P25205) DNA replication licensing factor MCM4 × 2 (P33991) DNA replication licensing factor MCM5 × 2 (P33992) DNA replication licensing factor MCM6 × 2 (Q14566) DNA replication licensing factor MCM7 × 2 (P33993) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 Author chain D; PDBConstruct 1–904; UniProt 1–904

Isoform 2 of DNA replication licensing factor MCM3

OrganismNot specified

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain 3; UniProt 1–853 Chain B; UniProt 1–853 Chain C; UniProt 1–853 Chain E; UniProt 1–853 Not recorded DNA replication licensing factor MCM2 × 2 (P49736) DNA replication licensing factor MCM4 × 2 (P33991) DNA replication licensing factor MCM5 × 2 (P33992) DNA replication licensing factor MCM6 × 2 (Q14566) DNA replication licensing factor MCM7 × 2 (P33993) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 P25205-2
PDB entities 2
Chains and sequence ranges Author chain 3; PDBConstruct 1–853; UniProt 1–853 Author chain B; PDBConstruct 1–853; UniProt 1–853 Author chain C; PDBConstruct 1–853; UniProt 1–853 Author chain E; PDBConstruct 1–853; UniProt 1–853

DNA replication licensing factor MCM4

OrganismNot specified

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain 4; UniProt 1–863 Chain F; UniProt 1–863 Not recorded DNA replication licensing factor MCM2 × 2 (P49736) Isoform 2 of DNA replication licensing factor MCM3 × 4 (P25205) DNA replication licensing factor MCM5 × 2 (P33992) DNA replication licensing factor MCM6 × 2 (Q14566) DNA replication licensing factor MCM7 × 2 (P33993) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 Author chain F; PDBConstruct 1–863; UniProt 1–863

DNA replication licensing factor MCM5

OrganismNot specified

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain 5; UniProt 1–734 Chain H; UniProt 1–734 Not recorded DNA replication licensing factor MCM2 × 2 (P49736) Isoform 2 of DNA replication licensing factor MCM3 × 4 (P25205) DNA replication licensing factor MCM4 × 2 (P33991) DNA replication licensing factor MCM6 × 2 (Q14566) DNA replication licensing factor MCM7 × 2 (P33993) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 Author chain H; PDBConstruct 1–734; UniProt 1–734

DNA replication licensing factor MCM6

OrganismNot specified

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain 6; UniProt 1–821 Chain G; UniProt 1–821 Not recorded DNA replication licensing factor MCM2 × 2 (P49736) Isoform 2 of DNA replication licensing factor MCM3 × 4 (P25205) DNA replication licensing factor MCM4 × 2 (P33991) DNA replication licensing factor MCM5 × 2 (P33992) DNA replication licensing factor MCM7 × 2 (P33993) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 Author chain G; PDBConstruct 1–821; UniProt 1–821

DNA replication licensing factor MCM7

OrganismNot specified

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain 7; UniProt 1–719 Chain A; UniProt 1–719 Not recorded DNA replication licensing factor MCM2 × 2 (P49736) Isoform 2 of DNA replication licensing factor MCM3 × 4 (P25205) DNA replication licensing factor MCM4 × 2 (P33991) DNA replication licensing factor MCM5 × 2 (P33992) DNA replication licensing factor MCM6 × 2 (Q14566) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 Author chain A; 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 9lxf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9lxf
Deposition date deposition_date2025-02-18
Structure title titleStructure of extended DNA-free MCM DH at 3.8 Angstroms resolution
Keywords keywordsMCM, Helicase, DNA replication, CELL CYCLE; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier82.45
Radius of gyration Rg (electron density) rg_electron82.86
Forward intensity I(0) i012539400000.00
Molecular weight molecular_weight941380.0 kDa
Excluded volume excluded_volume1175200 ų
Envelope volume envelope_volume1958500 ų
Hydration-shell volume shell_volume197590 ų
Envelope diameter envelope_diameter301.3
Shell Rg shell_rg81.50
Envelope Rg envelope_rg80.17
Shape Rg shape_rg82.88
Total Rg total_rg82.77
Total atoms total_atoms66032
Residues n_residues8310
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 dmax222.3
Rg (real space) rg_real79.64
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.2200e+10
I(0) uncertainty (real space) i0_real_error2.2180e+08
Rg (reciprocal space) rg_reciprocal80.74
I(0) (reciprocal space) i0_reciprocal12480000000.0000
Solution quality estimate total_estimate0.8739
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary81.9
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.622
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.1557
Highest regularization parameter α highest_alpha1175000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 0.979; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.007

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)