Research workbench
AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (B8CXE6)
Analyse AlphaFold monomer V2.0 prediction for histidine--tRNA ligase (B8CXE6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B8CXE6
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5ac15d0Cee6aab108aAE04D47EAea6219586a3F8
- Molecule
- Histidine--tRNA ligase
- UniProt
- B8CXE6
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine--tRNA ligase | protein | 419 | 43% helix, 21% strand | B8CXE6 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 632 | 0.76 | 0.82 | 61 | empty |
| 2 | 130 | 0.37 | 0.73 | 24 | empty |
| 3 | 59 | 0.31 | 0.75 | 17 | empty |
| 4 | 52 | 0.27 | 0.74 | 13 | 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 B8CXE6
- Elsewhere: UniProt B8CXE6 · AlphaFold DB B8CXE6
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