Research workbench
AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 12 (Q9D9M2)
Analyse AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 12… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9D9M2
- Type
- protein
- Length
- 370 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Ubiquitin carboxyl-terminal hydrolase 12
- UniProt
- Q9D9M2
- Pockets
- 3 · best druggability 0.55
Structure
1 distinct chain · 30% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin carboxyl-terminal hydrolase 12 | protein | 370 | 30% helix, 32% strand | Q9D9M2 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.55 | 0.89 | 14 | empty |
| 2 | 50 | 0.29 | 0.76 | 10 | empty |
| 3 | 53 | 0.28 | 0.75 | 11 | empty |
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 Q9D9M2
- Elsewhere: UniProt Q9D9M2 · AlphaFold DB Q9D9M2
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