9i3i

Cryo-EM structure of the MCM-ORC (MO) complex featuring an ORC2 regulatory domain involved in cell cycle regulation of MCM-DH loading for DNA replication.

Method: ELECTRON MICROSCOPY Dmax: 232.6 Å Quality: GOOD

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

Origin recognition complex subunit 1

Saccharomyces cerevisiae S288C

UniProt P54784

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: 14-meric(14) Consistent with all polymer counts Chain A; UniProt 1–914 Not recorded Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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.

25 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 36–949; UniProt 1–914

Origin recognition complex subunit 2

Saccharomyces cerevisiae S288C

UniProt P32833

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: 14-meric(14) Consistent with all polymer counts Chain B; UniProt 1–620 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–620; UniProt 1–620

Origin recognition complex subunit 3

Saccharomyces cerevisiae S288C

UniProt P54790

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: 14-meric(14) Consistent with all polymer counts Chain C; UniProt 1–616 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC3_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–616; UniProt 1–616

Origin recognition complex subunit 4

Saccharomyces cerevisiae S288C

UniProt P54791

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: 14-meric(14) Consistent with all polymer counts Chain D; UniProt 1–529 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC4_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–529; UniProt 1–529

Origin recognition complex subunit 5

Saccharomyces cerevisiae S288C

UniProt P50874

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: 14-meric(14) Consistent with all polymer counts Chain E; UniProt 1–479 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC5_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–479; UniProt 1–479

Origin recognition complex subunit 6

Saccharomyces cerevisiae S288C

UniProt P38826

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: 14-meric(14) Consistent with all polymer counts Chain F; UniProt 1–435 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC6_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–435; UniProt 1–435

DNA replication licensing factor MCM2

Saccharomyces cerevisiae 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: 14-meric(14) Consistent with all polymer counts Chain 2; UniProt 1–868 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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 7
Chains and sequence ranges Author chain 2; PDBConstruct 1–868; UniProt 1–868

DNA replication licensing factor MCM3

Saccharomyces cerevisiae 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: 14-meric(14) Consistent with all polymer counts Chain 3; UniProt 1–971 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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 8
Chains and sequence ranges Author chain 3; PDBConstruct 36–1006; UniProt 1–971

DNA replication licensing factor MCM4

Saccharomyces cerevisiae 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: 14-meric(14) Consistent with all polymer counts Chain 4; UniProt 1–933 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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 9
Chains and sequence ranges Author chain 4; PDBConstruct 1–933; UniProt 1–933

Minichromosome maintenance protein 5

Saccharomyces cerevisiae 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: 14-meric(14) Consistent with all polymer counts Chain 5; UniProt 1–775 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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 10
Chains and sequence ranges Author chain 5; PDBConstruct 1–775; UniProt 1–775

DNA replication licensing factor MCM6

Saccharomyces cerevisiae 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: 14-meric(14) Consistent with all polymer counts Chain 6; UniProt 1–1017 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM7 × 1 (P38132) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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 11
Chains and sequence ranges Author chain 6; PDBConstruct 1–1017; UniProt 1–1017

DNA replication licensing factor MCM7

Saccharomyces cerevisiae 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: 14-meric(14) Consistent with all polymer counts Chain 7; UniProt 1–845 Not recorded Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA (88-MER) × 1 DNA (88-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;10 second incubation, 3.5 seconds single side blotting. Resolution 4.40 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 12
Chains and sequence ranges Author chain 7; 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 9i3i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i3i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i3i
Deposition date deposition_date2025-01-23
Structure title titleCryo-EM structure of the MCM-ORC (MO) complex featuring an ORC2 regulatory domain involved in cell cycle regulation of MCM-DH loading for DNA replication.
Keywords keywordsDNA Replication, Origin licensing, MCM2-7 helicase, Origin Recognition Complex, CDK, cell cycle, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier83.85
Radius of gyration Rg (electron density) rg_electron85.25
Forward intensity I(0) i08737340000.00
Molecular weight molecular_weight765710.0 kDa
Excluded volume excluded_volume947110 ų
Envelope volume envelope_volume1590000 ų
Hydration-shell volume shell_volume161880 ų
Envelope diameter envelope_diameter290.4
Shell Rg shell_rg74.77
Envelope Rg envelope_rg83.17
Shape Rg shape_rg85.27
Total Rg total_rg85.07
Total atoms total_atoms105645
Residues n_residues6392
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 dmax232.6
Rg (real space) rg_real80.47
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real8.4160e+09
I(0) uncertainty (real space) i0_real_error1.6070e+08
Rg (reciprocal space) rg_reciprocal80.07
I(0) (reciprocal space) i0_reciprocal8643000000.0000
Solution quality estimate total_estimate0.8785
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.2
Skewness Skewness skewness0.476
Kurtosis Kurtosis kurtosis-0.711
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.8562
Highest regularization parameter α highest_alpha1625000000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.827; Stabil: 0.980; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.016

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

8. Citations (2)

9. Files and Curves (10)