2idc

Structure of the Histone H3-Asf1 Chaperone Interaction

Method: X-RAY DIFFRACTION Dmax: 68.5 Å Quality: GOOD

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

ANTI-SILENCING PROTEIN 1 AND HISTONE H3 CHIMERA

Saccharomyces cerevisiae

UniProt P32447

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–155 Fragment:Asf1, residues 2-155 and H3, residues 121-134 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;292 K;Tris-HCl, Li2SO4, PEG 4000, glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.20 Å R-free 0.239

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.

16 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASF1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–157; UniProt 2–155

ANTI-SILENCING PROTEIN 1 AND HISTONE H3 CHIMERA

Saccharomyces cerevisiae

UniProt P61830

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 122–135 Fragment:Asf1, residues 2-155 and H3, residues 121-134 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;292 K;Tris-HCl, Li2SO4, PEG 4000, glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.20 Å R-free 0.239

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.

37 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 166–179; UniProt 122–135

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 2idc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2idc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2idc
Deposition date deposition_date2006-09-14
Structure title titleStructure of the Histone H3-Asf1 Chaperone Interaction
Keywords keywordsIg-like fold, Asf1, H3, histone, chaperone, chromatin, Replication-Chaperone COMPLEX; Replication/Chaperone
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.54
Radius of gyration Rg (electron density) rg_electron17.52
Forward intensity I(0) i06418380.00
Molecular weight molecular_weight18923.0 kDa
Excluded volume excluded_volume23924 ų
Envelope volume envelope_volume28279 ų
Hydration-shell volume shell_volume14397 ų
Envelope diameter envelope_diameter69.0
Shell Rg shell_rg22.57
Envelope Rg envelope_rg18.05
Shape Rg shape_rg17.49
Total Rg total_rg18.49
Total atoms total_atoms1338
Residues n_residues167
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 dmax68.5
Rg (real space) rg_real18.63
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real6.4180e+06
I(0) uncertainty (real space) i0_real_error8.3020e+04
Rg (reciprocal space) rg_reciprocal18.62
I(0) (reciprocal space) i0_reciprocal6418000.0000
Solution quality estimate total_estimate0.8134
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.7
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis0.086
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2006000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.590; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.808; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2idca1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.22 — ASF1-like
Family Family familyb.1.22.1 — ASF1-like
Domain ID domain_idd2idca2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2idcA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1490 — Histone chaperone ASF1-like

8. Citations (1)

9. Files and Curves (10)