6eg2

Crystal structure of human BRM in complex with compound 16

Method: X-RAY DIFFRACTION Dmax: 95.5 Å Quality: EXCELLENT

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

Maltose/maltodextrin-binding periplasmic protein,Probable global transcription activator SNF2L2

Homo sapiens

UniProt P0AEY0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–392 Not recorded J7J N-(5-amino-2-chloropyridin-4-yl)-N'-(4-bromo-3-{[3-(hydroxymethyl)phenyl]ethynyl}-1,2-thiazol-5-yl)urea × 2 IPA ISOPROPYL ALCOHOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;100mM Hepes pH7.5, 200mM sodium chloride, 8% isopropanol Resolution 2.98 Å R-free 0.304

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.

109 other PDB entries and 148 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–366; UniProt 27–392

Maltose/maltodextrin-binding periplasmic protein,Probable global transcription activator SNF2L2

Homo sapiens

UniProt P51531

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 705–955 Not recorded J7J N-(5-amino-2-chloropyridin-4-yl)-N'-(4-bromo-3-{[3-(hydroxymethyl)phenyl]ethynyl}-1,2-thiazol-5-yl)urea × 2 IPA ISOPROPYL ALCOHOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;277 K;100mM Hepes pH7.5, 200mM sodium chloride, 8% isopropanol Resolution 2.98 Å R-free 0.304

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.

28 other PDB entries and 62 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMCA2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 371–621; UniProt 705–955

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 6eg2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6eg2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6eg2
Deposition date deposition_date2018-08-17
Structure title titleCrystal structure of human BRM in complex with compound 16
Keywords keywordsHelicase, ATPase, Chromatin remodeling, inhibitor, MBP fusion, Hydrolase-Hydrolase Inhibitor complex; Hydrolase/Hydrolase Inhibitor
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.32
Radius of gyration Rg (electron density) rg_electron29.45
Forward intensity I(0) i073161100.00
Molecular weight molecular_weight69877.0 kDa
Excluded volume excluded_volume88730 ų
Envelope volume envelope_volume114490 ų
Hydration-shell volume shell_volume32684 ų
Envelope diameter envelope_diameter100.0
Shell Rg shell_rg36.27
Envelope Rg envelope_rg29.16
Shape Rg shape_rg29.39
Total Rg total_rg30.34
Total atoms total_atoms4930
Residues n_residues619
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 dmax95.5
Rg (real space) rg_real30.27
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real7.3160e+07
I(0) uncertainty (real space) i0_real_error9.6290e+05
Rg (reciprocal space) rg_reciprocal30.29
I(0) (reciprocal space) i0_reciprocal73160000.0000
Solution quality estimate total_estimate0.9069
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-0.634
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15590000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6eg2A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily10810 — Tandem AAA-ATPase domain

8. Citations (1)

9. Files and Curves (10)