Research workbench
Crystal structure of S. aureus tars 217-571
Analyse Crystal structure of S. aureus tars 217-571 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U02
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl transferase
- EC
- 2.4.1.-
- UniProt
- A0A181F8T0
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycosyl transferase (EC 2.4.1.-) | protein | 355 | 27% helix, 39% strand | A0A181F8T0 |
Ligands and binding sites
- IMD · Imidazole · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.53 | 0.79 | 22 | empty |
| 2 | 58 | 0.52 | 0.86 | 12 | empty |
Compared structures
- 5U02 · Crystal structure of S. aureus TarS 217-571 · 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
- Every structure of UniProt A0A181F8T0
- Elsewhere: RCSB PDB 5U02 · PDBe 5U02 · UniProt A0A181F8T0
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