Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase, mitochondrial (P38714)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase, mitochondrial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P38714
- Type
- protein
- Length
- 643 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7f252798C74E00E84c69B04729dd9CAa146545FC
- Molecule
- Arginine--tRNA ligase, mitochondrial
- UniProt
- P38714
- Pockets
- 10 · best druggability 0.68
Structure
1 distinct chain · 57% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase, mitochondrial | protein | 643 | 57% helix, 10% strand | P38714 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.68 | 0.79 | 41 | empty |
| 2 | 347 | 0.66 | 0.80 | 36 | empty |
| 3 | 419 | 0.61 | 0.76 | 43 | empty |
| 4 | 267 | 0.56 | 0.77 | 37 | empty |
| 5 | 185 | 0.53 | 0.78 | 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 P38714
- Elsewhere: UniProt P38714 · AlphaFold DB P38714
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