Research workbench
AlphaFold monomer V2.0 prediction for mitochondrial-processing peptidase subunit beta (Q9CXT8)
Analyse AlphaFold monomer V2.0 prediction for mitochondrial-processing peptidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9CXT8
- Type
- protein
- Length
- 489 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x632101649E208e9BB842605138AfB7073cbac29F
- Molecule
- Mitochondrial-processing peptidase subunit beta
- UniProt
- Q9CXT8
- Pockets
- 4 · best druggability 0.74
Structure
1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial-processing peptidase subunit beta | protein | 489 | 45% helix, 17% strand | Q9CXT8 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1115 | 0.74 | 0.77 | 108 | empty |
| 2 | 94 | 0.40 | 0.77 | 19 | empty |
| 3 | 97 | 0.38 | 0.76 | 17 | empty |
| 4 | 89 | 0.38 | 0.76 | 21 | 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 Q9CXT8
- Elsewhere: UniProt Q9CXT8 · AlphaFold DB Q9CXT8
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