7y61

Cryo-EM structure of the two CAF1LCs bound right-handed Di-tetrasome

Method: ELECTRON MICROSCOPY Dmax: 129.3 Å Quality: GOOD

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

Histone H3.1

Homo sapiens

UniProt P68431

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain A; UniProt 1–136 Chain C; UniProt 1–136 Chain E; UniProt 1–136 Chain G; UniProt 1–136 Not recorded Histone H4 × 4 (P62805) Widom 601 DNA (147-MER) × 1 Widom 601 DNA (147-MER) × 1 Chromatin assembly factor 1 subunit A × 2 (Q13111) Chromatin assembly factor 1 subunit B × 2 (Q13112) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Hepes, pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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.

402 other PDB entries and 475 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–136; UniProt 1–136 Author chain C; PDBConstruct 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; UniProt 1–136 Author chain G; PDBConstruct 1–136; UniProt 1–136

Histone H4

Homo sapiens

UniProt P62805

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain B; UniProt 1–103 Chain D; UniProt 1–103 Chain F; UniProt 1–103 Chain H; UniProt 1–103 Not recorded Histone H3.1 × 4 (P68431) Widom 601 DNA (147-MER) × 1 Widom 601 DNA (147-MER) × 1 Chromatin assembly factor 1 subunit A × 2 (Q13111) Chromatin assembly factor 1 subunit B × 2 (Q13112) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Hepes, pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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.

581 other PDB entries and 633 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–103; UniProt 1–103 Author chain D; PDBConstruct 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103 Author chain H; PDBConstruct 1–103; UniProt 1–103

Chromatin assembly factor 1 subunit A

Homo sapiens

UniProt Q13111

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain K; UniProt 442–853 Chain M; UniProt 442–853 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Widom 601 DNA (147-MER) × 1 Widom 601 DNA (147-MER) × 1 Chromatin assembly factor 1 subunit B × 2 (Q13112) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Hepes, pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAF1A_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain K; PDBConstruct 1–412; UniProt 442–853 Author chain M; PDBConstruct 1–412; UniProt 442–853

Chromatin assembly factor 1 subunit B

Homo sapiens

UniProt Q13112

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 × 12 DNA 2 PDB declaration: tetradecameric(14) Consistent with all polymer counts Chain L; UniProt 1–419 Chain N; UniProt 1–419 Not recorded Histone H3.1 × 4 (P68431) Histone H4 × 4 (P62805) Widom 601 DNA (147-MER) × 1 Widom 601 DNA (147-MER) × 1 Chromatin assembly factor 1 subunit A × 2 (Q13111) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;20 mM Hepes, pH 7.5, 50 mM NaCl and 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAF1B_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain L; PDBConstruct 1–419; UniProt 1–419 Author chain N; PDBConstruct 1–419; UniProt 1–419

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 7y61

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7y61
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7y61
Deposition date deposition_date2022-06-18
Structure title titleCryo-EM structure of the two CAF1LCs bound right-handed Di-tetrasome
Keywords keywordsREPLICATION-DNA COMPLEX; REPLICATION/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.75
Radius of gyration Rg (electron density) rg_electron42.21
Forward intensity I(0) i0687422000.00
Molecular weight molecular_weight130270.0 kDa
Excluded volume excluded_volume126890 ų
Envelope volume envelope_volume300870 ų
Hydration-shell volume shell_volume61504 ų
Envelope diameter envelope_diameter137.0
Shell Rg shell_rg46.54
Envelope Rg envelope_rg39.60
Shape Rg shape_rg42.08
Total Rg total_rg42.59
Total atoms total_atoms8997
Residues n_residues1494
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 dmax129.3
Rg (real space) rg_real42.45
Rg uncertainty (real space) rg_real_error1.22
I(0) (real space) i0_real6.8740e+08
I(0) uncertainty (real space) i0_real_error1.2150e+07
Rg (reciprocal space) rg_reciprocal42.75
I(0) (reciprocal space) i0_reciprocal687600000.0000
Solution quality estimate total_estimate0.8816
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.4
Skewness Skewness skewness-0.018
Kurtosis Kurtosis kurtosis-0.431
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27570000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.850

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)