Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (O74017)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (O74017) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O74017
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x75B24D2B0e9632594da11Dd7fB5CA6a718195Fd6
- Molecule
- Peptidyl-tRNA hydrolase
- UniProt
- O74017
Structure
1 distinct chain · 43% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-tRNA hydrolase | protein | 121 | 43% helix, 26% strand | O74017 |
Compared structures
- 2D3K · Structural study on Project ID PH1539 from Pyrococcus horikoshii OT3 · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 2D3K · Structural study on project id PH1539 from pyrococcus horikoshii OT3 · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 1WN2 · Crystal structure of project ID PH1539 from Pyrococcus horikoshii OT3 · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 1WN2 · Crystal structure of project id PH1539 from pyrococcus horikoshii OT3 · an experimental structure of the same protein · chain A against A, TM-score 0.93
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 O74017
- Elsewhere: UniProt O74017 · AlphaFold DB O74017
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