Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A3DMF7)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (A3DMF7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3DMF7
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1613987cbC1744e137dAE77F5F9ad3696140470F
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- A3DMF7
Structure
1 distinct chain · 43% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 121 | 43% helix, 23% strand | A3DMF7 |
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 A3DMF7
- Elsewhere: UniProt A3DMF7 · AlphaFold DB A3DMF7
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