2grc

1.5 A structure of bromodomain from human BRG1 protein, a central ATPase of SWI/SNF remodeling complex

Method: X-RAY DIFFRACTION Dmax: 54.7 Å Quality: GOOD

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

Probable global transcription activator SNF2L4

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 1448–1575 Fragment:bromodomain, residues 1448-1575 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8.5;298 K;0.1 M Tris, 25% w/v PEG 3350, pH 8.5, VAPOR DIFFUSION, temperature 298.0K Resolution 1.50 Å R-free 0.264

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMCA4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–129; UniProt 1448–1575

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 2grc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2grc
Deposition date deposition_date2006-04-24
Structure title title1.5 A structure of bromodomain from human BRG1 protein, a central ATPase of SWI/SNF remodeling complex
Keywords keywordsBromodomain, BRG1, chromatin remodelling, acely-lysine binding, protein-protein interactions, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.35
Radius of gyration Rg (electron density) rg_electron15.08
Forward intensity I(0) i03706780.00
Molecular weight molecular_weight13954.0 kDa
Excluded volume excluded_volume17661 ų
Envelope volume envelope_volume20603 ų
Hydration-shell volume shell_volume11991 ų
Envelope diameter envelope_diameter55.3
Shell Rg shell_rg20.42
Envelope Rg envelope_rg15.60
Shape Rg shape_rg15.08
Total Rg total_rg16.21
Total atoms total_atoms982
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 dmax54.7
Rg (real space) rg_real16.32
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real3.7070e+06
I(0) uncertainty (real space) i0_real_error4.5510e+04
Rg (reciprocal space) rg_reciprocal16.32
I(0) (reciprocal space) i0_reciprocal3707000.0000
Solution quality estimate total_estimate0.8074
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.4
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.289
Angular range angular_range— – 0.4850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha457600.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2grca_
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_id2grcA00
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)