Research workbench
Crystal structure of thermus thermophilus valyl-tRNA synthetase complexed with TRNA(VAL) and valyl-adenylate analogue
Analyse Crystal structure of thermus thermophilus valyl-tRNA synthetase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GAX
- Type
- protein + RNA
- Length
- 1,876 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P96142
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | — | rna | 75 | — | — |
| A, B | — | protein | 863 | — | P96142 |
Compared structures
- 1GAX · Crystal structure of thermus thermophilus valyl-tRNA synthetase complexed with TRNA(VAL)… · the same entry in another collection · chain C against C, TM-score 1.00
- P96142 · AlphaFold monomer V2.0 prediction for valine--tRNA ligase (P96142) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P96142
- Elsewhere: RCSB PDB 1GAX · PDBe 1GAX · UniProt P96142
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