3c9c

Structural Basis of Histone H4 Recognition by p55

Method: X-RAY DIFFRACTION Dmax: 69.7 Å Quality: GOOD

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

Chromatin assembly factor 1 p55 subunit

Drosophila melanogaster

UniProt Q24572

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–430 Not recorded Histone H4, 27-residue peptide × 1 (P84040) CD CADMIUM ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Ammonium Sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.20 Å R-free 0.242

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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAF1_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–432; UniProt 1–430

Histone H4, 27-residue peptide

OrganismNot specified

UniProt P84040

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 16–42 Fragment:UNP residues 16-42 Chromatin assembly factor 1 p55 subunit × 1 (Q24572) CD CADMIUM ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;Ammonium Sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 3.20 Å R-free 0.242

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.

18 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–27; UniProt 16–42

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 3c9c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3c9c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3c9c
Deposition date deposition_date2008-02-15
Structure title titleStructural Basis of Histone H4 Recognition by p55
Keywords keywords;p55, chromatin, epigenetics, WD4, histone, Chromatin regulator, Nucleus, Phosphoprotein, Repressor, Transcription, Transcription regulation, WD repeat, Chromosomal protein, DNA-binding, Nucleosome core, NUCLEAR PROTEIN, TRANSCRIPTION REPRESSOR ;; TRANSCRIPTION REPRESSOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.13
Radius of gyration Rg (electron density) rg_electron21.02
Forward intensity I(0) i037886400.00
Molecular weight molecular_weight45324.0 kDa
Excluded volume excluded_volume55553 ų
Envelope volume envelope_volume65067 ų
Hydration-shell volume shell_volume25058 ų
Envelope diameter envelope_diameter71.1
Shell Rg shell_rg28.70
Envelope Rg envelope_rg21.51
Shape Rg shape_rg21.00
Total Rg total_rg21.99
Total atoms total_atoms3152
Residues n_residues391
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 dmax69.7
Rg (real space) rg_real21.99
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.7890e+07
I(0) uncertainty (real space) i0_real_error3.8970e+05
Rg (reciprocal space) rg_reciprocal22.02
I(0) (reciprocal space) i0_reciprocal37890000.0000
Solution quality estimate total_estimate0.8965
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-0.424
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7139000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3c9ca_
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.4 — WD40 repeat-like
Family Family familyb.69.4.1 — WD40-repeat

CATH v4.4 (1 domains)

Domain ID domain_id3c9cA00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)