5gjk

Crystal Structure of BAF47 and BAF155 Complex

Method: X-RAY DIFFRACTION Dmax: 57.0 Å Quality: REASONABLE

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

SWI/SNF complex subunit SMARCC1

Homo sapiens

UniProt Q92922

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 447–540 Fragment:UNP RESIDUES 447-540 SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 × 2 (Q12824) GOL GLYCEROL × 6 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 5.4;293 K;1 M sodium phosphate monobasic monohydrate, potassium phosphate dibasic, pH 5.4 Resolution 2.05 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.

4 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SMRC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–94; UniProt 447–540

SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1

Homo sapiens

UniProt Q12824

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 183–249 Fragment:UNP RESIDUES 183-249 SWI/SNF complex subunit SMARCC1 × 2 (Q92922) GOL GLYCEROL × 6 PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 5.4;293 K;1 M sodium phosphate monobasic monohydrate, potassium phosphate dibasic, pH 5.4 Resolution 2.05 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.

15 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNF5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–68; UniProt 183–249

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 5gjk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5gjk
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5gjk
Deposition date deposition_date2016-06-30
Structure title titleCrystal Structure of BAF47 and BAF155 Complex
Keywords keywordsComplex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.68
Radius of gyration Rg (electron density) rg_electron16.65
Forward intensity I(0) i06829090.00
Molecular weight molecular_weight19039.0 kDa
Excluded volume excluded_volume23777 ų
Envelope volume envelope_volume27320 ų
Hydration-shell volume shell_volume14149 ų
Envelope diameter envelope_diameter56.0
Shell Rg shell_rg22.02
Envelope Rg envelope_rg16.94
Shape Rg shape_rg16.65
Total Rg total_rg17.57
Total atoms total_atoms1337
Residues n_residues162
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 dmax57.0
Rg (real space) rg_real17.64
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real6.8290e+06
I(0) uncertainty (real space) i0_real_error7.5890e+04
Rg (reciprocal space) rg_reciprocal17.65
I(0) (reciprocal space) i0_reciprocal6829000.0000
Solution quality estimate total_estimate0.7319
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.0
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1604000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.994; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5gjka_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.1 — Homeodomain-like
Family Family familya.4.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id5gjkA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily10 — Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

8. Citations (1)

9. Files and Curves (10)