Research workbench
USP14 catalytic domain with IU1-248
Analyse USP14 catalytic domain with IU1-248 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IIN
- Type
- protein
- Length
- 671 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin carboxyl-terminal hydrolase 14
- EC
- 3.4.19.12
- UniProt
- P54578
- Ligands
- A8O
- Pockets
- 8 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) | protein | 336 | 29% helix, 31% strand | P54578 |
| B | Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) | protein | 335 | 31% helix, 28% strand | P54578 |
Ligands and binding sites
- A8O · 4-{3-[(4-hydroxypiperidin-1-yl)acetyl]-2,5-dimethyl-1H-pyrrol-1-yl}benzonitrile · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 90 | 0.52 | 0.84 | 17 | A8O |
| 2 | 61 | 0.51 | 0.86 | 17 | A8O |
| 3 | 146 | 0.43 | 0.75 | 19 | empty |
| 4 | 144 | 0.41 | 0.74 | 21 | empty |
| 5 | 95 | 0.41 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 759 Ų buried · 3 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 P54578
- Elsewhere: RCSB PDB 6IIN · PDBe 6IIN · UniProt P54578
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