Research workbench
Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA synthetase
Analyse Crystal structure of the aminoacylation catalytic fragment of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O5T
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophanyl-tRNA synthetase
- EC
- 6.1.1.2
- UniProt
- P23381
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophanyl-tRNA synthetase (EC 6.1.1.2) | protein | 378 | 54% helix, 10% strand | P23381 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 605 | 0.69 | 0.78 | 52 | empty |
| 2 | 239 | 0.56 | 0.78 | 25 | empty |
| 3 | 180 | 0.53 | 0.78 | 23 | empty |
Compared structures
- 1O5T · Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA… · the same entry in another collection · chain A against A, TM-score 1.00
- P23381 · AlphaFold monomer V2.0 prediction for tryptophan--tRNA ligase, cytoplasmic (P23381) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P23381
- Elsewhere: RCSB PDB 1O5T · PDBe 1O5T · UniProt P23381
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