Research workbench
Crystal structure of S. aureus tars
Analyse Crystal structure of S. aureus tars in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TZ8
- Type
- protein
- Length
- 1,674 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycosyl transferase
- EC
- 2.4.1.-
- UniProt
- A0A181F8T0
- Pockets
- 16 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B | Glycosyl transferase (EC 2.4.1.-) | protein | 558 | 28% helix, 33% strand | A0A181F8T0 |
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 843 | 0.85 | 0.87 | 84 | empty |
| 2 | 478 | 0.80 | 0.88 | 51 | empty |
| 3 | 559 | 0.64 | 0.76 | 44 | empty |
| 4 | 61 | 0.61 | 0.90 | 14 | empty |
| 5 | 72 | 0.57 | 0.87 | 18 | empty |
Interfaces
3 interfaces between chains.
- C–B · 1225 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1167 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 1150 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 5TZ8 · Crystal structure of S. aureus TarS · 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 5TZ8 · PDBe 5TZ8 · UniProt A0A181F8T0
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