9bcx

Cryo-EM structure of the S. cerevisiae ORC-Cdc6-Mcm2-7-DNA complex with a fully closed Mcm2-Mcm5 DNA entry gate

Method: ELECTRON MICROSCOPY Dmax: 185.6 Å Quality: GOOD

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

DNA replication licensing factor MCM2

Saccharomyces cerevisiae

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: 16-meric(16) Consistent with all polymer counts Chain 2; UniProt 1–868 Not recorded DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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

UniProt A0A8H8ULI2

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: 16-meric(16) Consistent with all polymer counts Chain 3; UniProt 1–971 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A8H8ULI2_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain 3; PDBConstruct 1–971; UniProt 1–971

DNA replication licensing factor MCM5

Saccharomyces cerevisiae

UniProt A0A6A5PUY8

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: 16-meric(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 (A0A8H8ULI2) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PUY8_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain 5; PDBConstruct 1–775; UniProt 1–775

DNA replication licensing factor MCM4

Saccharomyces cerevisiae

UniProt A0A8H4BU27

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: 16-meric(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 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A8H4BU27_YEASX
Isoform
PDB entities 4
Chains and sequence ranges Author chain 4; PDBConstruct 1–933; UniProt 1–933

DNA replication licensing factor MCM6

Saccharomyces cerevisiae

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: 16-meric(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 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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

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: 16-meric(16) Consistent with all polymer counts Chain 7; UniProt 1–845 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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 1–845; UniProt 1–845

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 × 14 DNA 2 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain B; UniProt 1–914 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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 7
Chains and sequence ranges Author chain B; PDBConstruct 1–914; UniProt 1–914

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 × 14 DNA 2 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain C; UniProt 1–620 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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 8
Chains and sequence ranges Author chain C; 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 × 14 DNA 2 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain D; UniProt 1–616 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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 9
Chains and sequence ranges Author chain D; PDBConstruct 1–616; UniProt 1–616

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 × 14 DNA 2 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain E; UniProt 1–529 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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 10
Chains and sequence ranges Author chain E; PDBConstruct 1–529; UniProt 1–529

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 × 14 DNA 2 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain F; UniProt 1–479 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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 11
Chains and sequence ranges Author chain F; PDBConstruct 1–479; UniProt 1–479

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 × 14 DNA 2 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain G; UniProt 1–435 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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 12
Chains and sequence ranges Author chain G; PDBConstruct 1–435; UniProt 1–435

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 × 14 DNA 2 PDB declaration: 16-meric(16) Consistent with all polymer counts Chain I; UniProt 1–513 Not recorded DNA replication licensing factor MCM2 × 1 (P29469) DNA replication licensing factor MCM3 × 1 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) TAH11 isoform 1 × 1 (A0A8H4C095) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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 13
Chains and sequence ranges Author chain I; PDBConstruct 1–513; UniProt 1–513

TAH11 isoform 1

Saccharomyces cerevisiae

UniProt A0A8H4C095

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: 16-meric(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 (A0A8H8ULI2) DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) DNA replication licensing factor MCM4 × 1 (A0A8H4BU27) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) 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) Cell division control protein 6 × 1 (P09119) DNA (39-MER) × 1 DNA (39-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.10 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A8H4C095_YEASX
Isoform
PDB entities 14
Chains and sequence ranges Author chain 8; PDBConstruct 1–604; UniProt 1–604

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 9bcx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9bcx
Deposition date deposition_date2024-04-10
Structure title titleCryo-EM structure of the S. cerevisiae ORC-Cdc6-Mcm2-7-DNA complex with a fully closed Mcm2-Mcm5 DNA entry gate
Keywords keywordsDNA replication, Cryo-EM, OCCM-deltaC6, REPLICATION-DNA complex, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.50
Radius of gyration Rg (electron density) rg_electron65.29
Forward intensity I(0) i09418050000.00
Molecular weight molecular_weight818750.0 kDa
Excluded volume excluded_volume1023500 ų
Envelope volume envelope_volume1673000 ų
Hydration-shell volume shell_volume200720 ų
Envelope diameter envelope_diameter213.4
Shell Rg shell_rg74.61
Envelope Rg envelope_rg63.92
Shape Rg shape_rg65.32
Total Rg total_rg65.33
Total atoms total_atoms57494
Residues n_residues7165
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 dmax185.6
Rg (real space) rg_real65.13
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real9.4170e+09
I(0) uncertainty (real space) i0_real_error1.7170e+08
Rg (reciprocal space) rg_reciprocal65.77
I(0) (reciprocal space) i0_reciprocal9428000000.0000
Solution quality estimate total_estimate0.8399
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary77.3
Skewness Skewness skewness0.214
Kurtosis Kurtosis kurtosis-0.477
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha2104000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.982; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

8. Citations (1)

9. Files and Curves (10)