Research workbench
AlphaFold monomer V2.0 prediction for peptide deformylase (C0M9E1)
Analyse AlphaFold monomer V2.0 prediction for peptide deformylase (C0M9E1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C0M9E1
- Type
- protein
- Length
- 204 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x979789353e6255fD1B9686ec8eB84C4662C56FCd
- Molecule
- Peptide deformylase
- UniProt
- C0M9E1
- Pockets
- 1 · best druggability 0.54
Structure
1 distinct chain · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide deformylase | protein | 204 | 27% helix, 25% strand | C0M9E1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.54 | 0.82 | 20 | 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 C0M9E1
- Elsewhere: UniProt C0M9E1 · AlphaFold DB C0M9E1
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