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The crystal structure of aaleurs-CP1-D20
Analyse The crystal structure of aaleurs-CP1-D20 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PZ5
- Type
- protein
- Length
- 383 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 0.58
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucyl-tRNA synthetase subunit alpha (EC 6.1.1.4) | protein | 191 | 32% helix, 24% strand | O66680 |
| B | Leucyl-tRNA synthetase subunit alpha (EC 6.1.1.4) | protein | 192 | 32% 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 | 237 | 0.58 | 0.79 | 24 | empty |
| 2 | 224 | 0.56 | 0.79 | 24 | empty |
| 3 | 250 | 0.53 | 0.76 | 39 | empty |
| 4 | 51 | 0.25 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 214 Ų buried · 6 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 O66680
- Elsewhere: RCSB PDB 3PZ5 · PDBe 3PZ5 · UniProt O66680
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