Research workbench
USP14 catalytic domain bind to IU1-47
Analyse USP14 catalytic domain bind to IU1-47 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IIL
- Type
- protein
- Length
- 673 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
- A8F
- Pockets
- 7 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) | protein | 341 | 32% helix, 31% strand | P54578 |
| B | Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) | protein | 332 | 33% helix, 29% strand | P54578 |
Ligands and binding sites
- A8F · 1-[1-(4-chlorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-2-(piperidin-1-yl)ethan-1-one · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.55 | 0.86 | 15 | A8F |
| 2 | 76 | 0.51 | 0.84 | 15 | A8F |
| 3 | 121 | 0.48 | 0.79 | 25 | empty |
| 4 | 198 | 0.48 | 0.76 | 26 | empty |
| 5 | 176 | 0.46 | 0.75 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 768 Ų buried · 2 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 6IIL · PDBe 6IIL · UniProt P54578
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