Research workbench
Crystal structure of the fourth bromodomain of human poly-bromodomain containing protein 1 (PB1)
Analyse Crystal structure of the fourth bromodomain of human poly-bromodomain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TLP
- Type
- protein
- Length
- 236 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein polybromo-1
- UniProt
- Q86U86
- Ligands
- NI
- Pockets
- 5 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein polybromo-1 | protein | 119 | 67% helix, 2% strand | Q86U86 |
| B | Protein polybromo-1 | protein | 117 | 65% helix, 2% strand | Q86U86 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.49 | 0.84 | 16 | empty |
| 2 | 90 | 0.49 | 0.82 | 15 | empty |
| 3 | 76 | 0.47 | 0.82 | 15 | empty |
| 4 | 123 | 0.42 | 0.75 | 25 | empty |
| 5 | 65 | 0.27 | 0.72 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 231 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3TLP · Crystal structure of the fourth bromodomain of human poly-bromodomain containing protein… · the same entry in another collection · chain A against A, TM-score 1.00
- Q86U86 · AlphaFold monomer V2.0 prediction for protein polybromo-1 (Q86U86) · 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 Q86U86
- Elsewhere: RCSB PDB 3TLP · PDBe 3TLP · UniProt Q86U86
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