7qhs

S. cerevisiae CMGE nucleating origin DNA melting

Method: ELECTRON MICROSCOPY Dmax: 213.8 Å Quality: GOOD

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

DNA replication licensing factor MCM2

Saccharomyces cerevisiae

UniProt A0A6A5Q1S9

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 × 13 DNA 2 PDB declaration: pentadecameric(15) 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) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q1S9_YEASX
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 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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain 3; UniProt 1–971 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 2
Chains and sequence ranges Author chain 3; PDBConstruct 36–1006; UniProt 1–971

DNA replication licensing factor MCM4

Saccharomyces cerevisiae

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain 4; UniProt 1–933 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain 6; UniProt 1–1017 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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 4
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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain 7; UniProt 1–845 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 5
Chains and sequence ranges Author chain 7; PDBConstruct 1–845; UniProt 1–845

DNA replication complex GINS protein PSF1

Saccharomyces cerevisiae

UniProt A0A6A5Q203

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain H; UniProt 1–208 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name A0A6A5Q203_YEASX
Isoform
PDB entities 6
Chains and sequence ranges Author chain H; PDBConstruct 1–208; UniProt 1–208

DNA replication complex GINS protein PSF2

Saccharomyces cerevisiae

UniProt A0A6A5PX40

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain I; UniProt 1–213 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name A0A6A5PX40_YEASX
Isoform
PDB entities 7
Chains and sequence ranges Author chain I; PDBConstruct 1–213; UniProt 1–213

DNA replication complex GINS protein PSF3

Saccharomyces cerevisiae

UniProt Q12146

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain C; UniProt 1–194 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSF3_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain C; PDBConstruct 36–229; UniProt 1–194

DNA replication complex GINS protein SLD5

Saccharomyces cerevisiae

UniProt Q03406

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain D; UniProt 1–294 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

33 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SLD5_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain D; PDBConstruct 1–294; UniProt 1–294

Cell division control protein 45

Saccharomyces cerevisiae

UniProt Q08032

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain E; UniProt 1–650 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

34 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC45_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain E; PDBConstruct 1–657; UniProt 1–650

DNA polymerase epsilon subunit B

Saccharomyces cerevisiae

UniProt P24482

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain F; UniProt 1–689 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 DPB2_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain F; PDBConstruct 1–689; UniProt 1–689

DNA polymerase epsilon catalytic subunit A

Saccharomyces cerevisiae

UniProt P21951

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain G; UniProt 1–2222 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA (26-MER) × 1 DNA (26-MER) × 1 DNA replication licensing factor MCM5 × 1 (A0A6A5PUY8) ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

33 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPOE_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain G; PDBConstruct 1–2222; UniProt 1–2222

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 × 13 DNA 2 PDB declaration: pentadecameric(15) Consistent with all polymer counts Chain 5; UniProt 1–775 Not recorded DNA replication licensing factor MCM2 × 1 (A0A6A5Q1S9) DNA replication licensing factor MCM3 × 1 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication licensing factor MCM7 × 1 (P38132) DNA replication complex GINS protein PSF1 × 1 (A0A6A5Q203) DNA replication complex GINS protein PSF2 × 1 (A0A6A5PX40) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase epsilon subunit B × 1 (P24482) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA (26-MER) × 1 DNA (26-MER) × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ZN ZINC ION × 7 MG MAGNESIUM ION × 3 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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 15
Chains and sequence ranges Author chain 5; PDBConstruct 1–775; UniProt 1–775

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 7qhs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qhs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qhs
Deposition date deposition_date2021-12-14
Structure title titleS. cerevisiae CMGE nucleating origin DNA melting
Keywords keywordsDNA replication, helicase, initiation, DNA origin, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.80
Radius of gyration Rg (electron density) rg_electron63.82
Forward intensity I(0) i08237760000.00
Molecular weight molecular_weight764840.0 kDa
Excluded volume excluded_volume956410 ų
Envelope volume envelope_volume1469400 ų
Hydration-shell volume shell_volume182860 ų
Envelope diameter envelope_diameter220.5
Shell Rg shell_rg71.21
Envelope Rg envelope_rg62.79
Shape Rg shape_rg63.84
Total Rg total_rg63.89
Total atoms total_atoms53670
Residues n_residues6616
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 dmax213.8
Rg (real space) rg_real63.58
Rg uncertainty (real space) rg_real_error1.80
I(0) (real space) i0_real8.2380e+09
I(0) uncertainty (real space) i0_real_error1.8020e+08
Rg (reciprocal space) rg_reciprocal63.96
I(0) (reciprocal space) i0_reciprocal8243000000.0000
Solution quality estimate total_estimate0.8596
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.0
Skewness Skewness skewness0.294
Kurtosis Kurtosis kurtosis-0.318
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1548000000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.815; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.768

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (19)

8. Citations (1)

9. Files and Curves (10)