Research workbench
Tyrosyl-tRNA synthetase from thermus thermophilus complexed with wild- type TRNATYR(GUA) and with ATP and tyrosinol
Analyse Tyrosyl-tRNA synthetase from thermus thermophilus complexed with wild- type… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H3E
- Type
- protein + RNA
- Length
- 511 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P83453
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 428 | — | P83453 |
| B | — | rna | 83 | — | — |
Compared structures
- 1H3E · Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with wild-type tRNAtyr(GUA)… · the same entry in another collection · chain A against A, TM-score 1.00
- P83453 · AlphaFold monomer V2.0 prediction for tyrosine--tRNA ligase (P83453) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 P83453
- Elsewhere: RCSB PDB 1H3E · PDBe 1H3E · UniProt P83453
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