4qyd

Crystal Structure of the human BRPF1 bromodomain in complex with a histone H4K12ac peptide

Method: X-RAY DIFFRACTION Dmax: 54.1 Å Quality: GOOD

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

Peregrin

Homo sapiens

UniProt P55201

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 629–742 Fragment:bromodomain (UNP residues 629-742) Histone H4 × 1 (P62805) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;277 K;0.1 M HEPES, pH 7.5, 10% w/v polyethylene glycol (PEG) 6,000, 5% v/v (+/-)-2-methyl-2,4-pentanediol (MPD), VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.94 Å R-free 0.213

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.

64 other PDB entries and 94 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BRPF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–117; UniProt 629–742

Histone H4

OrganismNot specified

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 5–18 Fragment:histone H4K12ac peptide (UNP residues 5-18) Non-standard monomer:Yes (specific site not provided by mmCIF) Peregrin × 1 (P55201) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;277 K;0.1 M HEPES, pH 7.5, 10% w/v polyethylene glycol (PEG) 6,000, 5% v/v (+/-)-2-methyl-2,4-pentanediol (MPD), VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.94 Å R-free 0.213

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 1–14; UniProt 5–18

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 4qyd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qyd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4qyd
Deposition date deposition_date2014-07-24
Structure title titleCrystal Structure of the human BRPF1 bromodomain in complex with a histone H4K12ac peptide
Keywords keywords;bromodomain-PHD finger protein 1 (BRPF1), histone acetyltransferase (HAT), monocytic leukemia zinc-finger (MOZ), epigenetics, chromatin reader, bromodomain, histone post-transcriptional modification (PTM) reader domain, histone H4 acetylated at lysine 14, acetyllysine, nucleus, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.08
Radius of gyration Rg (electron density) rg_electron15.05
Forward intensity I(0) i03869700.00
Molecular weight molecular_weight14117.0 kDa
Excluded volume excluded_volume17788 ų
Envelope volume envelope_volume20748 ų
Hydration-shell volume shell_volume12056 ų
Envelope diameter envelope_diameter53.6
Shell Rg shell_rg20.27
Envelope Rg envelope_rg15.49
Shape Rg shape_rg15.02
Total Rg total_rg16.20
Total atoms total_atoms995
Residues n_residues121
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 dmax54.1
Rg (real space) rg_real16.08
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real3.8700e+06
I(0) uncertainty (real space) i0_real_error5.1000e+04
Rg (reciprocal space) rg_reciprocal16.08
I(0) (reciprocal space) i0_reciprocal3870000.0000
Solution quality estimate total_estimate0.7884
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.5
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.198
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha953800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.757; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4qydA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily10 — Bromodomain-like

8. Citations (1)

9. Files and Curves (10)