Research workbench
AlphaFold monomer V2.0 prediction for methionine aminopeptidase 2-2 (Q0CL94)
Analyse AlphaFold monomer V2.0 prediction for methionine aminopeptidase 2-2 (Q0CL94) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0CL94
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Methionine aminopeptidase 2-2
- UniProt
- Q0CL94
- Pockets
- 4 · best druggability 0.43
Structure
1 distinct chain · 29% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine aminopeptidase 2-2 | protein | 445 | 29% helix, 21% strand | Q0CL94 |
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 | 120 | 0.43 | 0.77 | 24 | empty |
| 2 | 134 | 0.43 | 0.76 | 29 | empty |
| 3 | 111 | 0.40 | 0.75 | 23 | empty |
| 4 | 55 | 0.24 | 0.72 | 12 | 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 Q0CL94
- Elsewhere: UniProt Q0CL94 · AlphaFold DB Q0CL94
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