Research workbench
Crystal structure of the USP15 dusp-ubl monomer
Analyse Crystal structure of the USP15 dusp-ubl monomer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A3O
- Type
- protein
- Length
- 423 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin carboxyl-terminal hydrolase 15
- EC
- 3.4.19.12
- UniProt
- Q9Y4E8
- Pockets
- 3 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) | protein | 211 | 24% helix, 29% strand | Q9Y4E8 |
| B | Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) | protein | 212 | 24% helix, 26% strand | Q9Y4E8 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.32 | 0.73 | 14 | GOL |
| 2 | 59 | 0.29 | 0.74 | 17 | empty |
| 3 | 51 | 0.25 | 0.72 | 17 | GOL |
Interfaces
1 interface between chains.
- A–B · 145 Ų buried · 1 hydrogen bond · 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 Q9Y4E8
- Elsewhere: RCSB PDB 4A3O · PDBe 4A3O · UniProt Q9Y4E8
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