8s0d

H. sapiens MCM bound to double stranded DNA and ORC1-6

Method: ELECTRON MICROSCOPY Dmax: 237.0 Å Quality: GOOD

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

Origin recognition complex subunit 6

Homo sapiens

UniProt Q9Y5N6

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: tetradecameric(14) Consistent with all polymer counts Chain F; UniProt 2–252 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) DNA replication licensing factor MCM7 × 1 (P33993) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–251; UniProt 2–252

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain 2; UniProt 1–902 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–902; UniProt 1–902

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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain 3; UniProt 1–808 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 3
Chains and sequence ranges Author chain 3; PDBConstruct 3–810; 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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain 4; UniProt 1–863 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 4
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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain 5; UniProt 1–734 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 5
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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain 6; UniProt 1–821 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 6
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–DNA Heteromer Protein × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain 7; UniProt 1–719 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 7
Chains and sequence ranges Author chain 7; PDBConstruct 1–719; UniProt 1–719

Origin recognition complex subunit 1

Homo sapiens

UniProt Q13415

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: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 1–861 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA replication licensing factor MCM7 × 1 (P33993) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

12 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC1_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain A; PDBConstruct 1–861; UniProt 1–861

Origin recognition complex subunit 2

Homo sapiens

UniProt Q13416

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: tetradecameric(14) Consistent with all polymer counts Chain B; UniProt 1–577 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA replication licensing factor MCM7 × 1 (P33993) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

15 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC2_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain B; PDBConstruct 1–577; UniProt 1–577

Isoform 2 of Origin recognition complex subunit 3

Homo sapiens

UniProt Q9UBD5

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: tetradecameric(14) Consistent with all polymer counts Chain C; UniProt 1–712 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA replication licensing factor MCM7 × 1 (P33993) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Origin recognition complex subunit 4 × 1 (O43929) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

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

View Construct and Data Evidence
UniProt name ORC3_HUMAN
Isoform Q9UBD5-2
PDB entities 12
Chains and sequence ranges Author chain C; PDBConstruct 1–712; UniProt 1–712

Origin recognition complex subunit 4

Homo sapiens

UniProt O43929

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: tetradecameric(14) Consistent with all polymer counts Chain D; UniProt 1–436 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA replication licensing factor MCM7 × 1 (P33993) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 5 × 1 (O43913) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC4_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain D; PDBConstruct 1–436; UniProt 1–436

Origin recognition complex subunit 5

Homo sapiens

UniProt O43913

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: tetradecameric(14) Consistent with all polymer counts Chain E; UniProt 1–435 Not recorded Origin recognition complex subunit 6 × 1 (Q9Y5N6) 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) DNA replication licensing factor MCM7 × 1 (P33993) DNA (58-mer) × 1 DNA (58-mer) × 1 Origin recognition complex subunit 1 × 1 (Q13415) Origin recognition complex subunit 2 × 1 (Q13416) Isoform 2 of Origin recognition complex subunit 3 × 1 (Q9UBD5) Origin recognition complex subunit 4 × 1 (O43929) AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 5 MG MAGNESIUM ION × 8 ZN ZINC ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ORC5_HUMAN
Isoform
PDB entities 14
Chains and sequence ranges Author chain E; PDBConstruct 1–435; UniProt 1–435

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 8s0d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8s0d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8s0d
Deposition date deposition_date2024-02-13
Structure title titleH. sapiens MCM bound to double stranded DNA and ORC1-6
Keywords keywordsAAA+ ATPase, DNA helicase, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.25
Radius of gyration Rg (electron density) rg_electron67.79
Forward intensity I(0) i06496050000.00
Molecular weight molecular_weight658220.0 kDa
Excluded volume excluded_volume814930 ų
Envelope volume envelope_volume1337000 ų
Hydration-shell volume shell_volume163920 ų
Envelope diameter envelope_diameter237.4
Shell Rg shell_rg68.51
Envelope Rg envelope_rg65.82
Shape Rg shape_rg67.85
Total Rg total_rg67.60
Total atoms total_atoms46024
Residues n_residues5539
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 dmax237.0
Rg (real space) rg_real67.28
Rg uncertainty (real space) rg_real_error2.39
I(0) (real space) i0_real6.4960e+09
I(0) uncertainty (real space) i0_real_error1.3420e+08
Rg (reciprocal space) rg_reciprocal67.01
I(0) (reciprocal space) i0_reciprocal6492000000.0000
Solution quality estimate total_estimate0.8476
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary72.1
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha1276000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.727; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.835

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

8. Citations (3)

9. Files and Curves (10)