Research workbench
Human BRD2(BD2) mutant in free form
Analyse Human BRD2(BD2) mutant in free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5O38
- Type
- protein
- Length
- 113 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bromodomain-containing protein 2
- UniProt
- P25440
- Ligands
- 9JB, DQW, CL
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bromodomain-containing protein 2 | protein | 113 | 66% helix, 0% strand | P25440 |
Ligands and binding sites
- 9JB · 3-[(2~{R})-2-oxidanylpropoxy]-2-[[(2~{R})-2-oxidanylpropoxy]methyl]-2-[[(2~{S})-2-oxidanylpropoxy]methyl]propan-1-ol · ligand · chains A
- DQW · (2~{S})-1-[(2~{S})-2-oxidanylpropoxy]propan-2-ol · ligand · chains A
- CL · Chloride ion · ion · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.52 | 0.81 | 18 | 9JB |
Compared structures
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 P25440
- Elsewhere: RCSB PDB 5O38 · PDBe 5O38 · UniProt P25440
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.