Research workbench
AlphaFold monomer V2.0 prediction for mitochondrial inner membrane protease subunit 1 (Q96LU5)
Analyse AlphaFold monomer V2.0 prediction for mitochondrial inner membrane protease… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96LU5
- Type
- protein
- Length
- 166 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- Mitochondrial inner membrane protease subunit 1
- UniProt
- Q96LU5
- Pockets
- 1 · best druggability 0.34
Structure
1 distinct chain · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial inner membrane protease subunit 1 | protein | 166 | 28% helix, 30% strand | Q96LU5 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.34 | 0.77 | 18 | 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 Q96LU5
- Elsewhere: UniProt Q96LU5 · AlphaFold DB Q96LU5
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