5eps

Crystal structure of the human BRPF1 bromodomain in complex with SEED10

Method: X-RAY DIFFRACTION Dmax: 52.0 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 627–740 Fragment:UNP residues 625-740 5QX 1-methyl-3,4-dihydroquinoxalin-2-one × 1 NO3 NITRATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;0.1 M Sodium Acetate, pH5.5, 0.15 M Sodium Nitrate, 20% PEG3350 Resolution 1.47 Å R-free 0.198

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 3–116; UniProt 627–740

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 5eps

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5eps
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5eps
Deposition date deposition_date2015-11-12
Structure title titleCrystal structure of the human BRPF1 bromodomain in complex with SEED10
Keywords keywords;Bromodomain and PHD finger-containing protein 1(BRPF1), monocytic leukemia zinc-finger (MOZ), Inhibitor, transcription, DNA binding protein ;; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.65
Radius of gyration Rg (electron density) rg_electron14.67
Forward intensity I(0) i03536340.00
Molecular weight molecular_weight13479.0 kDa
Excluded volume excluded_volume16941 ų
Envelope volume envelope_volume19290 ų
Hydration-shell volume shell_volume11586 ų
Envelope diameter envelope_diameter52.3
Shell Rg shell_rg19.77
Envelope Rg envelope_rg15.03
Shape Rg shape_rg14.65
Total Rg total_rg15.77
Total atoms total_atoms950
Residues n_residues113
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 dmax52.0
Rg (real space) rg_real15.64
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.5360e+06
I(0) uncertainty (real space) i0_real_error3.5870e+04
Rg (reciprocal space) rg_reciprocal15.64
I(0) (reciprocal space) i0_reciprocal3536000.0000
Solution quality estimate total_estimate0.7944
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.145
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha697000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.778; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5epsa_
Class classa — All alpha proteins
Fold Fold folda.29 — Bromodomain-like
Superfamily Superfamily superfamilya.29.2 — Bromodomain
Family Family familya.29.2.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id5epsA00
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)