8z50

Crystal structure of the ASF1-H3T-H4 complex

Method: X-RAY DIFFRACTION Dmax: 73.0 Å Quality: GOOD

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

Histone chaperone ASF1A

Homo sapiens

UniProt Q9Y294

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–173 Not recorded Histone H3.1t × 1 (Q16695) Histone H4 × 1 (P62805) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;1.0 M Lithium chloride, 0.1 M MES pH 6.0, 10% PEG 6000 Resolution 2.80 Å R-free 0.255

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.

17 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASF1A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–173; UniProt 1–173

Histone H3.1t

Homo sapiens

UniProt Q16695

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–136 Not recorded Histone chaperone ASF1A × 1 (Q9Y294) Histone H4 × 1 (P62805) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;1.0 M Lithium chloride, 0.1 M MES pH 6.0, 10% PEG 6000 Resolution 2.80 Å R-free 0.255

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.

12 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31T_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–103 Not recorded Histone chaperone ASF1A × 1 (Q9Y294) Histone H3.1t × 1 (Q16695) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;1.0 M Lithium chloride, 0.1 M MES pH 6.0, 10% PEG 6000 Resolution 2.80 Å R-free 0.255

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 C; PDBConstruct 1–103; UniProt 1–103

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 8z50

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8z50
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8z50
Deposition date deposition_date2024-04-18
Structure title titleCrystal structure of the ASF1-H3T-H4 complex
Keywords keywordsASF1, histone, H3-H4, H3T, H2A-H2B, Nucleosome, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.30
Radius of gyration Rg (electron density) rg_electron21.30
Forward intensity I(0) i020142400.00
Molecular weight molecular_weight34794.0 kDa
Excluded volume excluded_volume43898 ų
Envelope volume envelope_volume53023 ų
Hydration-shell volume shell_volume21032 ų
Envelope diameter envelope_diameter75.5
Shell Rg shell_rg27.67
Envelope Rg envelope_rg21.52
Shape Rg shape_rg21.27
Total Rg total_rg22.26
Total atoms total_atoms2452
Residues n_residues304
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 dmax73.0
Rg (real space) rg_real22.25
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real2.0140e+07
I(0) uncertainty (real space) i0_real_error2.6330e+05
Rg (reciprocal space) rg_reciprocal22.27
I(0) (reciprocal space) i0_reciprocal20140000.0000
Solution quality estimate total_estimate0.8947
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.506
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7520000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)