6skl

Cryo-EM structure of the CMG Fork Protection Complex at a replication fork - Conformation 1

Method: ELECTRON MICROSCOPY Dmax: 263.0 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 × 16 DNA 2 PDB declaration: octadecameric(18) 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 × 16 DNA 2 PDB declaration: octadecameric(18) 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 × 16 DNA 2 PDB declaration: octadecameric(18) 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 × 16 DNA 2 PDB declaration: octadecameric(18) 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 × 16 DNA 2 PDB declaration: octadecameric(18) 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 × 16 DNA 2 PDB declaration: octadecameric(18) 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 (strain ATCC 204508 / 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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain A; UniProt 1–208 Fragment:Tof1 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 (strain ATCC 204508 / 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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain B; UniProt 1–213 Fragment:Csm3 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 (strain ATCC 204508 / 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 × 16 DNA 2 PDB declaration: octadecameric(18) 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 24–217; UniProt 1–194

DNA replication complex GINS protein SLD5

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain D; UniProt 1–294 Fragment:Ctf4 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 (strain ATCC 204508 / 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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain E; UniProt 1–650 Fragment:Mcm4 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 (strain ATCC 204508 / 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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain F; UniProt 1–927 Chain G; UniProt 1–927 Chain H; UniProt 1–927 Fragment:Mcm6 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 (strain ATCC 204508 / 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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain X; UniProt 1–1238 Fragment:Mcm2 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Chromosome segregation in meiosis protein 3 × 1 (Q04659) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 X; PDBConstruct 1–1238; UniProt 1–1238

Chromosome segregation in meiosis protein 3

Saccharomyces cerevisiae (strain ATCC 204508 / 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 × 16 DNA 2 PDB declaration: octadecameric(18) Consistent with all polymer counts Chain Y; UniProt 1–317 Fragment:Mcm3 Mutation:CBP-tag at N-terminus 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 fork, leading-strand template × 1 DNA fork, lagging-strand template × 1 Topoisomerase 1-associated factor 1 × 1 (P53840) ZN ZINC ION × 5 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Three microlitres of sample was applied on a grid and incubated for 15-30 s at 4 degC before manually blotting with filter paper for 10 s and plunge-freezing in liquid ethane. Resolution 3.70 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 Y; PDBConstruct 1–317; UniProt 1–317

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 6skl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6skl
Deposition date deposition_date2019-08-16
Structure title titleCryo-EM structure of the CMG Fork Protection Complex at a replication fork - Conformation 1
Keywords keywordsprotein-DNA complex, replisome, AAA+ helicase, CMG, GINS, fork DNA, MCM, fork protection complex, CIP-box, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.69
Radius of gyration Rg (electron density) rg_electron70.90
Forward intensity I(0) i09861150000.00
Molecular weight molecular_weight842580.0 kDa
Excluded volume excluded_volume1055000 ų
Envelope volume envelope_volume1616900 ų
Hydration-shell volume shell_volume185870 ų
Envelope diameter envelope_diameter253.3
Shell Rg shell_rg73.91
Envelope Rg envelope_rg69.63
Shape Rg shape_rg70.95
Total Rg total_rg70.78
Total atoms total_atoms118220
Residues n_residues7310
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 dmax263.0
Rg (real space) rg_real74.75
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real9.9360e+09
I(0) uncertainty (real space) i0_real_error1.9180e+08
Rg (reciprocal space) rg_reciprocal70.52
I(0) (reciprocal space) i0_reciprocal9857000000.0000
Solution quality estimate total_estimate0.8788
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary83.7
Skewness Skewness skewness0.581
Kurtosis Kurtosis kurtosis0.079
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.9776
Highest regularization parameter α highest_alpha1297000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.750; Stabil: 0.848; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.685

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (19)

8. Citations (1)

9. Files and Curves (10)