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Crystal structure of arginyl-tRNA synthetase
Analyse Crystal structure of arginyl-tRNA synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q2Y
- Type
- protein
- Length
- 1,142 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginine--tRNA ligase, cytoplasmic
- EC
- 6.1.1.19
- UniProt
- P54136
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) | protein | 565 | 50% helix, 10% strand | P54136 |
| B | Arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) | protein | 577 | 52% helix, 11% strand | P54136 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 689 | 0.74 | 0.80 | 44 | empty |
| 2 | 332 | 0.68 | 0.82 | 43 | empty |
| 3 | 553 | 0.63 | 0.75 | 44 | empty |
| 4 | 301 | 0.63 | 0.80 | 41 | empty |
| 5 | 522 | 0.62 | 0.75 | 42 | empty |
Interfaces
1 interface between chains.
- A–B · 1236 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 P54136
- Elsewhere: RCSB PDB 4Q2Y · PDBe 4Q2Y · UniProt P54136
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