Research workbench
Crystal structure of heterotetrameric complex of yoeb-yefm toxin- antitoxin from staphylococcus aureus.
Analyse Crystal structure of heterotetrameric complex of yoeb-yefm toxin- antitoxin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L8F
- Type
- protein
- Length
- 682 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Yoeb; Antitoxin
- UniProt
- Q2G286, Q2G285
- Pockets
- 8 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 49% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, C, H, G | Yoeb | protein | 87 | 38% helix, 29% strand | Q2G286 |
| B, E | Antitoxin | protein | 83 | 55% helix, 23% strand | Q2G285 |
| A, F | Antitoxin | protein | 84 | 55% helix, 23% strand | Q2G285 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 661 | 0.69 | 0.77 | 67 | empty |
| 2 | 138 | 0.50 | 0.79 | 19 | empty |
| 3 | 118 | 0.43 | 0.77 | 21 | empty |
| 4 | 98 | 0.35 | 0.74 | 18 | empty |
| 5 | 75 | 0.31 | 0.74 | 11 | empty |
Interfaces
20 interfaces between chains.
- G–E · 1726 Ų buried · 35 hydrogen bonds · protein-protein
- B–A · 1726 Ų buried · 19 hydrogen bonds · protein-protein
- C–A · 1725 Ų buried · 36 hydrogen bonds · protein-protein
- H–F · 1702 Ų buried · 37 hydrogen bonds · protein-protein
- D–B · 1689 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 6L8F · Crystal structure of heterotetrameric complex of YoeB-YefM toxin-antitoxin from… · the same entry in another collection · chain D against D, 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 Q2G286
- Every structure of UniProt Q2G285
- Elsewhere: RCSB PDB 6L8F · PDBe 6L8F · UniProt Q2G286 · UniProt Q2G285
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