Research workbench
Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub- complexes
Analyse Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HSN
- Type
- protein
- Length
- 280 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00958, P46672
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 160 | — | P00958 |
| B | — | protein | 120 | — | P46672 |
Compared structures
- 2HSN · Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal… · the same entry in another collection · chain A against A, TM-score 1.00
- P46672 · AlphaFold monomer V2.0 prediction for tRNA-aminoacylation cofactor ARC1 (P46672) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P00958
- Every structure of UniProt P46672
- Elsewhere: RCSB PDB 2HSN · PDBe 2HSN · UniProt P00958 · UniProt P46672
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