Research workbench
Crystal structure of the second bromodomain of human polybromo
Analyse Crystal structure of the second bromodomain of human polybromo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LJW
- Type
- protein
- Length
- 238 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein polybromo-1
- UniProt
- Q86U86
- Ligands
- NA
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein polybromo-1 | protein | 118 | 66% helix, 2% strand | Q86U86 |
| B | Protein polybromo-1 | protein | 120 | 65% helix, 2% strand | Q86U86 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 377 | 0.60 | 0.76 | 53 | empty |
| 2 | 80 | 0.53 | 0.84 | 15 | empty |
| 3 | 88 | 0.50 | 0.82 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 379 Ų buried · 6 hydrogen bonds · protein-protein
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 Q86U86
- Elsewhere: RCSB PDB 3LJW · PDBe 3LJW · UniProt Q86U86
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