Research workbench
Crystal structure of BAZ2A bromodomain in complex with 4-propionyl- pyrrole derivative 2
Analyse Crystal structure of BAZ2A bromodomain in complex with 4-propionyl- pyrrole… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MGK
- Type
- protein
- Length
- 103 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain adjacent to zinc finger domain protein 2A
- UniProt
- Q9UIF9
- Ligands
- 7MW
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain adjacent to zinc finger domain protein 2A | protein | 103 | 64% helix, 0% strand | Q9UIF9 |
Ligands and binding sites
- 7MW · methyl 4-propanoyl-1~{H}-pyrrole-2-carboxylate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.47 | 0.83 | 18 | 7MW |
Compared structures
- 5MGK · Crystal Structure of BAZ2A bromodomain in complex with 4-propionyl-pyrrole derivative 2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UIF9 · AlphaFold monomer V2.0 prediction for bromodomain adjacent to zinc finger domain protein… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9UIF9
- Elsewhere: RCSB PDB 5MGK · PDBe 5MGK · UniProt Q9UIF9
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