5dkd

Crystal structure of the bromodomain of human BRG1 (SMARCA4) in complex with PFI-3 chemical probe

Method: X-RAY DIFFRACTION Dmax: 68.1 Å Quality: GOOD

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

Transcription activator BRG1

Homo sapiens

UniProt P51532

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 1418–1536 Fragment:UNP residues 1418-1536 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 3 5BW (2E)-1-(2-hydroxyphenyl)-3-[(1R,4R)-5-(pyridin-2-yl)-2,5-diazabicyclo[2.2.1]hept-2-yl]prop-2-en-1-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;277.15 K;0.1 M Bis Tris pH 7.2, 0.1 M ammonium acetate, 0.1 M ZnCl2, 15% PEG smear high (mixture from PEG8k to 20k) Resolution 2.00 Å R-free 0.297
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1418–1536 Fragment:UNP residues 1418-1536 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 3 5BW (2E)-1-(2-hydroxyphenyl)-3-[(1R,4R)-5-(pyridin-2-yl)-2,5-diazabicyclo[2.2.1]hept-2-yl]prop-2-en-1-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.2;277.15 K;0.1 M Bis Tris pH 7.2, 0.1 M ammonium acetate, 0.1 M ZnCl2, 15% PEG smear high (mixture from PEG8k to 20k) Resolution 2.00 Å R-free 0.297

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.

25 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMCA4_HUMAN
Isoform P51532-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–121; UniProt 1418–1536 Author chain B; PDBConstruct 3–121; UniProt 1418–1536

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 5dkd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5dkd
Deposition date deposition_date2015-09-03
Structure title titleCrystal structure of the bromodomain of human BRG1 (SMARCA4) in complex with PFI-3 chemical probe
Keywords keywordsSWI-SNF complex, chromatin remodeling, Brg associated factors (BAF), transcription, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.00
Radius of gyration Rg (electron density) rg_electron20.07
Forward intensity I(0) i012195600.00
Molecular weight molecular_weight27129.0 kDa
Excluded volume excluded_volume34502 ų
Envelope volume envelope_volume42541 ų
Hydration-shell volume shell_volume18097 ų
Envelope diameter envelope_diameter71.7
Shell Rg shell_rg25.97
Envelope Rg envelope_rg20.06
Shape Rg shape_rg20.07
Total Rg total_rg21.00
Total atoms total_atoms1901
Residues n_residues220
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 dmax68.1
Rg (real space) rg_real20.96
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.2200e+07
I(0) uncertainty (real space) i0_real_error1.5830e+05
Rg (reciprocal space) rg_reciprocal20.97
I(0) (reciprocal space) i0_reciprocal12200000.0000
Solution quality estimate total_estimate0.8208
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.485
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2453000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5dkda_
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
Domain ID domain_idd5dkdb_
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 (2 domains)

Domain ID domain_id5dkdA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology920 — Histone Acetyltransferase; Chain A
Homologous superfamily homologous superfamily10 — Bromodomain-like
Domain ID domain_id5dkdB00
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)