Research workbench
Solution structure of the tgs domain from human threonyl-tRNA synthetase
Analyse Solution structure of the tgs domain from human threonyl-tRNA synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WWT
- Type
- protein
- Length
- 88 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Threonyl-tRNA synthetase, cytoplasmic
- EC
- 6.1.1.3
- UniProt
- P26639
Structure
solution nmr · 1 distinct chain · 11% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Threonyl-tRNA synthetase, cytoplasmic (EC 6.1.1.3) | protein | 88 | 11% helix, 23% strand | P26639 |
Compared structures
- 1WWT · Solution structure of the TGS domain from human threonyl-tRNA synthetase · the same entry in another collection · chain A against A, TM-score 1.00
- P26639 · AlphaFold monomer V2.0 prediction for threonine--tRNA ligase 1, cytoplasmic (P26639) · a predicted model of the same protein · chain A against A, TM-score 0.79
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 P26639
- Elsewhere: RCSB PDB 1WWT · PDBe 1WWT · UniProt P26639
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