MolNFT v1 · #73379 · protein
Crystal structure of the wild type CP1 hydrolitic domain from aquifex aeolicus leucyl-tRNA
3O0A · Leucyl-tRNA synthetase subunit alpha: “Crystal structure of the wild type CP1 hydrolitic domain from aquifex aeolicus leucyl-tRNA”. X-ray diffraction, 4 pockets (best druggability 0.71). MolNFT v1 #73379 on GenesisL1: 3D structure…
- PDB
- 3O0A
- Type
- protein
- Length
- 425 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucyl-tRNA synthetase subunit alpha
- EC
- 6.1.1.4
- UniProt
- O66680
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucyl-tRNA synthetase subunit alpha (EC 6.1.1.4) | protein | 211 | 36% helix, 23% strand | O66680 |
| B | Leucyl-tRNA synthetase subunit alpha (EC 6.1.1.4) | protein | 214 | 36% helix, 23% strand | O66680 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.71 | 0.81 | 50 | empty |
| 2 | 170 | 0.52 | 0.79 | 30 | empty |
| 3 | 179 | 0.51 | 0.78 | 25 | empty |
| 4 | 81 | 0.38 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 372 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3O0A · Crystal structure of the wild type CP1 hydrolitic domain from Aquifex Aeolicus leucyl-trna · the same entry in another collection · chain A against A, TM-score 1.00
- O66680 · AlphaFold monomer V2.0 prediction for leucine--tRNA ligase subunit alpha (O66680) · a predicted model of the same protein · chain A 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 O66680
- Elsewhere: RCSB PDB 3O0A · PDBe 3O0A · UniProt O66680
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