5v8f

Structural basis of MCM2-7 replicative helicase loading by ORC-Cdc6 and Cdt1

Method: ELECTRON MICROSCOPY Dmax: 210.5 Å Quality: GOOD

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

DNA replication licensing factor MCM2

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain 2; UniProt 1–868 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 1
Chains and sequence ranges Author chain 2; PDBConstruct 1–868; UniProt 1–868

DNA replication licensing factor MCM3

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain 3; UniProt 1–971 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 2
Chains and sequence ranges Author chain 3; PDBConstruct 1–971; UniProt 1–971

DNA replication licensing factor MCM4

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain 4; UniProt 1–933 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 3
Chains and sequence ranges Author chain 4; PDBConstruct 1–933; UniProt 1–933

Minichromosome maintenance protein 5

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain 5; UniProt 1–775 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 4
Chains and sequence ranges Author chain 5; PDBConstruct 1–775; UniProt 1–775

DNA replication licensing factor MCM6

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain 6; UniProt 1–1017 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 5
Chains and sequence ranges Author chain 6; PDBConstruct 1–1017; UniProt 1–1017

DNA replication licensing factor MCM7

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain 7; UniProt 1–800 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 6
Chains and sequence ranges Author chain 7; PDBConstruct 1–800; UniProt 1–800

Cell division cycle protein CDT1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P47112

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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain 8; UniProt 1–604 Not recorded 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) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

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

View Construct and Data Evidence
UniProt name CDT1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain 8; PDBConstruct 1–604; UniProt 1–604

Cell division control protein 6

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain 9; UniProt 1–513 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 8
Chains and sequence ranges Author chain 9; PDBConstruct 1–513; UniProt 1–513

Origin recognition complex subunit 1

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain A; UniProt 1–913 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 9
Chains and sequence ranges Author chain A; PDBConstruct 1–913; UniProt 1–913

Origin recognition complex subunit 2

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain B; UniProt 1–620 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 10
Chains and sequence ranges Author chain B; PDBConstruct 1–620; UniProt 1–620

Origin recognition complex subunit 3

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain C; UniProt 1–616 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 11
Chains and sequence ranges Author chain C; PDBConstruct 1–616; UniProt 1–616

Origin recognition complex subunit 5

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain E; UniProt 1–479 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 12
Chains and sequence ranges Author chain E; PDBConstruct 1–479; UniProt 1–479

Origin recognition complex subunit 4

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain D; UniProt 1–529 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 13
Chains and sequence ranges Author chain D; PDBConstruct 1–529; UniProt 1–529

Origin recognition complex subunit 6

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 14 DNA 2 PDB declaration: hexadecameric(16) Consistent with all polymer counts Chain F; UniProt 1–435 Not recorded 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) Cell division cycle protein CDT1 × 1 (P47112) 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 (39-MER) × 1 DNA (39-MER) × 1 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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 14
Chains and sequence ranges Author chain F; 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 5v8f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5v8f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5v8f
Deposition date deposition_date2017-03-21
Structure title titleStructural basis of MCM2-7 replicative helicase loading by ORC-Cdc6 and Cdt1
Keywords keywordsDNA replication, Cryo-EM, OCCM, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.23
Radius of gyration Rg (electron density) rg_electron64.15
Forward intensity I(0) i010172000000.00
Molecular weight molecular_weight849350.0 kDa
Excluded volume excluded_volume1061400 ų
Envelope volume envelope_volume1597400 ų
Hydration-shell volume shell_volume195430 ų
Envelope diameter envelope_diameter209.1
Shell Rg shell_rg73.53
Envelope Rg envelope_rg62.51
Shape Rg shape_rg64.19
Total Rg total_rg64.13
Total atoms total_atoms59586
Residues n_residues7296
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 dmax210.5
Rg (real space) rg_real63.83
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real1.0170e+10
I(0) uncertainty (real space) i0_real_error1.8850e+08
Rg (reciprocal space) rg_reciprocal64.53
I(0) (reciprocal space) i0_reciprocal10180000000.0000
Solution quality estimate total_estimate0.8670
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.0
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0005
Highest regularization parameter α highest_alpha1845000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.766

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5v8f601
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1640 — mini-chromosome maintenance (MCM) complex, chain A, domain 1
Homologous superfamily homologous superfamily10 — mini-chromosome maintenance (MCM) complex, chain A, domain 1
Domain ID domain_id5v8f604
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5v8f701
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5v8fE01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)