7y5v

Cryo-EM structure of the dimeric human CAF1LC-H3-H4 complex

Method: ELECTRON MICROSCOPY Dmax: 160.3 Å Quality: GOOD

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

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 442–853 Chain F; UniProt 442–853 Not recorded Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone-binding protein RBBP4 × 2 (Q09028) 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 6.10 Å

Other States of the Same Protein in the Database

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

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–412; UniProt 442–853 Author chain F; PDBConstruct 1–412; UniProt 442–853

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 1–136 Chain I; UniProt 1–136 Not recorded Chromatin assembly factor 1 subunit A × 2 (Q13111) Histone H4 × 2 (P62805) Histone-binding protein RBBP4 × 2 (Q09028) 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 6.10 Å

Other States of the Same Protein in the Database

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

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 2
Chains and sequence ranges Author chain D; PDBConstruct 1–136; UniProt 1–136 Author chain I; 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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 1–103 Chain J; UniProt 1–103 Not recorded Chromatin assembly factor 1 subunit A × 2 (Q13111) Histone H3.1 × 2 (P68431) Histone-binding protein RBBP4 × 2 (Q09028) 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 6.10 Å

Other States of the Same Protein in the Database

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

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 3
Chains and sequence ranges Author chain E; PDBConstruct 1–103; UniProt 1–103 Author chain J; PDBConstruct 1–103; UniProt 1–103

Histone-binding protein RBBP4

Homo sapiens

UniProt Q09028

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 1–425 Chain H; UniProt 1–425 Not recorded Chromatin assembly factor 1 subunit A × 2 (Q13111) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) 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 6.10 Å

Other States of the Same Protein in the Database

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

49 other PDB entries and 69 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBBP4_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–425; UniProt 1–425 Author chain H; PDBConstruct 1–425; UniProt 1–425

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 heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain B; UniProt 1–419 Chain G; UniProt 1–419 Not recorded Chromatin assembly factor 1 subunit A × 2 (Q13111) Histone H3.1 × 2 (P68431) Histone H4 × 2 (P62805) Histone-binding protein RBBP4 × 2 (Q09028) 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 6.10 Å

Other States of the Same Protein in the Database

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

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 5
Chains and sequence ranges Author chain B; PDBConstruct 1–419; UniProt 1–419 Author chain G; 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 7y5v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7y5v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7y5v
Deposition date deposition_date2022-06-17
Structure title titleCryo-EM structure of the dimeric human CAF1LC-H3-H4 complex
Keywords keywordsHistone chaperone, Chromatin assembly factor, REPLICATION; REPLICATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.52
Radius of gyration Rg (electron density) rg_electron48.53
Forward intensity I(0) i0633161000.00
Molecular weight molecular_weight127600.0 kDa
Excluded volume excluded_volume125410 ų
Envelope volume envelope_volume355700 ų
Hydration-shell volume shell_volume64699 ų
Envelope diameter envelope_diameter156.8
Shell Rg shell_rg49.31
Envelope Rg envelope_rg46.17
Shape Rg shape_rg48.54
Total Rg total_rg48.55
Total atoms total_atoms9104
Residues n_residues2276
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 dmax160.3
Rg (real space) rg_real48.54
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real6.3320e+08
I(0) uncertainty (real space) i0_real_error1.2310e+07
Rg (reciprocal space) rg_reciprocal48.53
I(0) (reciprocal space) i0_reciprocal633100000.0000
Solution quality estimate total_estimate0.8799
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.1
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.571
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha108400000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.688

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)