Research workbench
AlphaFold monomer V2.0 prediction for mitochondrial outer membrane protein porin 1 (Q9SRH5)
Analyse AlphaFold monomer V2.0 prediction for mitochondrial outer membrane protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9SRH5
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- Mitochondrial outer membrane protein porin 1
- UniProt
- Q9SRH5
- Pockets
- 4 · best druggability 0.43
Structure
1 distinct chain · 7% helix, 64% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial outer membrane protein porin 1 | protein | 276 | 7% helix, 64% strand | Q9SRH5 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.43 | 0.77 | 17 | empty |
| 2 | 94 | 0.38 | 0.76 | 26 | empty |
| 3 | 101 | 0.36 | 0.74 | 19 | empty |
| 4 | 73 | 0.30 | 0.74 | 19 | 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 Q9SRH5
- Elsewhere: UniProt Q9SRH5 · AlphaFold DB Q9SRH5
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