Research workbench
Crystal structure of S. aureus tyrrs in complex with SB284485
Analyse Crystal structure of S. aureus tyrrs in complex with SB284485 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JIL
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosyl-tRNA synthetase
- EC
- 6.1.1.1
- Ligands
- 485
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosyl-tRNA synthetase (EC 6.1.1.1) | protein | 323 | 57% helix, 11% strand | — |
Ligands and binding sites
- 485 · [2-amino-3-(4-hydroxy-phenyl)-propionylamino]- (3,4,5-trihydroxy-6-methyl-tetrahydro-pyran-2-yl)- acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 368 | 0.70 | 0.83 | 43 | 485 |
| 2 | 126 | 0.41 | 0.75 | 18 | empty |
Compared structures
- 1JIL · Crystal structure of S. aureus TyrRS in complex with SB284485 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 1JIL · PDBe 1JIL
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