8kg6

Yeast replisome in state I

Method: ELECTRON MICROSCOPY Dmax: 275.9 Å Quality: GOOD

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

DNA replication licensing factor MCM2

Saccharomyces cerevisiae 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 × 18 DNA 2 PDB declaration: 20-meric(20) 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 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 × 18 DNA 2 PDB declaration: 20-meric(20) 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 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 × 18 DNA 2 PDB declaration: 20-meric(20) 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 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 × 18 DNA 2 PDB declaration: 20-meric(20) 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 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 × 18 DNA 2 PDB declaration: 20-meric(20) 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 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 × 18 DNA 2 PDB declaration: 20-meric(20) 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 (P24279) DNA replication licensing factor MCM4 × 1 (P30665) Minichromosome maintenance protein 5 × 1 (P29496) DNA replication licensing factor MCM6 × 1 (P53091) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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

DNA replication complex GINS protein PSF1

Saccharomyces cerevisiae S288C

UniProt Q12488

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain A; UniProt 1–208 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) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSF1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain A; PDBConstruct 1–208; UniProt 1–208

DNA replication complex GINS protein PSF2

Saccharomyces cerevisiae S288C

UniProt P40359

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain B; UniProt 1–213 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSF2_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain B; PDBConstruct 1–213; UniProt 1–213

DNA replication complex GINS protein PSF3

Saccharomyces cerevisiae S288C

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain C; UniProt 1–194 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA polymerase alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 9
Chains and sequence ranges Author chain C; PDBConstruct 1–194; UniProt 1–194

DNA replication complex GINS protein SLD5

Saccharomyces cerevisiae S288C

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain D; UniProt 1–294 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) Cell division control protein 45 × 1 (Q08032) DNA polymerase alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 10
Chains and sequence ranges Author chain D; PDBConstruct 1–294; UniProt 1–294

Cell division control protein 45

Saccharomyces cerevisiae S288C

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain E; UniProt 1–650 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) DNA polymerase alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 11
Chains and sequence ranges Author chain E; PDBConstruct 1–650; UniProt 1–650

DNA polymerase alpha-binding protein

Saccharomyces cerevisiae S288C

UniProt Q01454

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain F; UniProt 1–927 Chain G; UniProt 1–927 Chain H; UniProt 1–927 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) DNA replication complex GINS protein PSF3 × 1 (Q12146) DNA replication complex GINS protein SLD5 × 1 (Q03406) Cell division control protein 45 × 1 (Q08032) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 CTF4_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain F; PDBConstruct 1–927; UniProt 1–927 Author chain G; PDBConstruct 1–927; UniProt 1–927 Author chain H; PDBConstruct 1–927; UniProt 1–927

Topoisomerase 1-associated factor 1

Saccharomyces cerevisiae S288C

UniProt P53840

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain K; UniProt 1–1238 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOF1_YEAST
Isoform
PDB entities 15
Chains and sequence ranges Author chain K; PDBConstruct 1–1238; UniProt 1–1238

Chromosome segregation in meiosis protein 3

Saccharomyces cerevisiae S288C

UniProt Q04659

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain L; UniProt 1–317 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) DNA polymerase epsilon catalytic subunit A × 1 (P21951) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 CSM3_YEAST
Isoform
PDB entities 16
Chains and sequence ranges Author chain L; PDBConstruct 1–317; UniProt 1–317

DNA polymerase epsilon catalytic subunit A

Saccharomyces cerevisiae S288C

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain M; UniProt 1–2222 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon subunit B × 1 (P24482) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 17
Chains and sequence ranges Author chain M; PDBConstruct 1–2222; UniProt 1–2222

DNA polymerase epsilon subunit B

Saccharomyces cerevisiae S288C

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 × 18 DNA 2 PDB declaration: 20-meric(20) Consistent with all polymer counts Chain N; UniProt 1–689 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) DNA replication complex GINS protein PSF1 × 1 (Q12488) DNA replication complex GINS protein PSF2 × 1 (P40359) 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 alpha-binding protein × 3 (Q01454) DNA (71-mer) × 1 DNA (61-mer) × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) DNA polymerase epsilon catalytic subunit A × 1 (P21951) ZN ZINC ION × 7 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 5 AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;blot with filter paper for 3-4 seconds before plunging. Resolution 3.07 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 18
Chains and sequence ranges Author chain N; PDBConstruct 1–689; UniProt 1–689

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 8kg6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8kg6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8kg6
Deposition date deposition_date2023-08-17
最后修订 last_revision2023-12-06
Structure title titleYeast replisome in state I
Keywords keywordsreplisome, complex, DNA replication, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier74.16
Radius of gyration Rg (electron density) rg_electron74.36
Forward intensity I(0) i013875400000.00
Molecular weight molecular_weight1005000.0 kDa
Excluded volume excluded_volume1259800 ų
Envelope volume envelope_volume1903700 ų
Hydration-shell volume shell_volume209320 ų
Envelope diameter envelope_diameter249.6
Shell Rg shell_rg76.18
Envelope Rg envelope_rg73.34
Shape Rg shape_rg74.41
Total Rg total_rg74.22
Total atoms total_atoms70613
Residues n_residues8760
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 dmax275.9
Rg (real space) rg_real78.30
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real1.3970e+10
I(0) uncertainty (real space) i0_real_error2.8330e+08
Rg (reciprocal space) rg_reciprocal74.23
I(0) (reciprocal space) i0_reciprocal13880000000.0000
Solution quality estimate total_estimate0.8861
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary78.8
Skewness Skewness skewness0.559
Kurtosis Kurtosis kurtosis0.115
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.9636
Highest regularization parameter α highest_alpha1572000000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.758; Stabil: 0.851; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.745

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (22)

8. Citations (1)

9. Files and Curves (10)