Research workbench
Crystal structure of the bromodomain of human transcription activator BRG1 (SMARCA4) in complex with 2-(6-amino-5-(piperazin-1-yl) pyridazin-3-YL)PHENOL
Analyse Crystal structure of the bromodomain of human transcription activator BRG1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZS2
- Type
- protein
- Length
- 242 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription activator BRG1
- EC
- 3.6.4.-
- UniProt
- P51532
- Ligands
- FX5
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Transcription activator BRG1 (EC 3.6.4.-) | protein | 121 | 60% helix, 2% strand | P51532 |
Ligands and binding sites
- FX5 · 2-(6-azanyl-5-piperazin-4-ium-1-yl-pyridazin-3-yl) phenol · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.46 | 0.83 | 15 | FX5 |
| 2 | 58 | 0.45 | 0.83 | 15 | FX5 |
| 3 | 97 | 0.34 | 0.73 | 19 | empty |
| 4 | 56 | 0.25 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 89 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6ZS2 · Crystal Structure of the bromodomain of human transcription activator BRG1 (SMARCA4) in… · the same entry in another collection · chain A against A, TM-score 1.00
- P51532 · AlphaFold monomer V2.0 prediction for transcription activator BRG1 (P51532) · a predicted model of the same protein · chain A against A, TM-score 0.96
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P51532
- Elsewhere: RCSB PDB 6ZS2 · PDBe 6ZS2 · UniProt P51532
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