6wgc

Atomic model of semi-attached mutant OCCM-DNA complex (ORC-Cdc6-Cdt1-Mcm2-7 with Mcm6 WHD truncation)

Method: ELECTRON MICROSCOPY Dmax: 158.6 Å Quality: GOOD

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

Cell division control protein 6

Saccharomyces cerevisiae

UniProt P09119

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain 9; UniProt 1–513 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 4 × 1 (P54791) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM7 × 1 (P38132) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC6_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain 9; PDBConstruct 1–513; UniProt 1–513

Origin recognition complex subunit 1

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain A; UniProt 1–913 Not recorded Cell division control protein 6 × 1 (P09119) 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 4 × 1 (P54791) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM7 × 1 (P38132) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–913; UniProt 1–913

Origin recognition complex subunit 2

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain B; UniProt 1–620 Not recorded Cell division control protein 6 × 1 (P09119) Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 3 × 1 (P54790) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM7 × 1 (P38132) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 3
Chains and sequence ranges Author chain B; PDBConstruct 1–620; UniProt 1–620

Origin recognition complex subunit 3

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain C; UniProt 1–616 Not recorded Cell division control protein 6 × 1 (P09119) Origin recognition complex subunit 1 × 1 (P54784) Origin recognition complex subunit 2 × 1 (P32833) Origin recognition complex subunit 5 × 1 (P50874) Origin recognition complex subunit 4 × 1 (P54791) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM7 × 1 (P38132) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 4
Chains and sequence ranges Author chain C; PDBConstruct 1–616; UniProt 1–616

Origin recognition complex subunit 5

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain E; UniProt 1–479 Not recorded Cell division control protein 6 × 1 (P09119) 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 MCM3 × 1 (P24279) DNA replication licensing factor MCM7 × 1 (P38132) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 4

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain D; UniProt 1–529 Not recorded Cell division control protein 6 × 1 (P09119) 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 MCM3 × 1 (P24279) DNA replication licensing factor MCM7 × 1 (P38132) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 6
Chains and sequence ranges Author chain D; PDBConstruct 1–529; UniProt 1–529

Origin recognition complex subunit 6

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain F; UniProt 1–435 Not recorded Cell division control protein 6 × 1 (P09119) 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 4 × 1 (P54791) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM7 × 1 (P38132) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 7
Chains and sequence ranges Author chain F; PDBConstruct 1–435; UniProt 1–435

DNA replication licensing factor MCM3

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain 3; UniProt 1–971 Not recorded Cell division control protein 6 × 1 (P09119) 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 4 × 1 (P54791) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM7 × 1 (P38132) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 1–971; UniProt 1–971

DNA replication licensing factor MCM7

Saccharomyces cerevisiae

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 × 9 DNA 2 PDB declaration: undecameric(11) Consistent with all polymer counts Chain 7; UniProt 1–845 Not recorded Cell division control protein 6 × 1 (P09119) 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 4 × 1 (P54791) Origin recognition complex subunit 6 × 1 (P38826) DNA replication licensing factor MCM3 × 1 (P24279) DNA (41-MER) × 1 DNA (41-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 9
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 6wgc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6wgc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6wgc
Deposition date deposition_date2020-04-05
Structure title titleAtomic model of semi-attached mutant OCCM-DNA complex (ORC-Cdc6-Cdt1-Mcm2-7 with Mcm6 WHD truncation)
Keywords keywordsDNA replication, Cryo-EM, OCCM-deltaC6, REPLICATION-DNA complex; REPLICATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.74
Radius of gyration Rg (electron density) rg_electron47.75
Forward intensity I(0) i01837570000.00
Molecular weight molecular_weight351270.0 kDa
Excluded volume excluded_volume437230 ų
Envelope volume envelope_volume626390 ų
Hydration-shell volume shell_volume105230 ų
Envelope diameter envelope_diameter172.1
Shell Rg shell_rg54.89
Envelope Rg envelope_rg47.20
Shape Rg shape_rg47.77
Total Rg total_rg47.91
Total atoms total_atoms24605
Residues n_residues2886
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 dmax158.6
Rg (real space) rg_real47.55
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real1.8380e+09
I(0) uncertainty (real space) i0_real_error3.9040e+07
Rg (reciprocal space) rg_reciprocal47.74
I(0) (reciprocal space) i0_reciprocal1838000000.0000
Solution quality estimate total_estimate0.8712
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.7
Skewness Skewness skewness0.283
Kurtosis Kurtosis kurtosis-0.262
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha344800000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.891

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)