Research workbench
S. aureus mepr G34R mutant
Analyse S. aureus mepr G34R mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F6F
- Type
- protein
- Length
- 282 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Marr family regulatory protein
- UniProt
- Q5Y812
- Pockets
- 2 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Marr family regulatory protein | protein | 141 | 69% helix, 8% strand | Q5Y812 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.40 | 0.74 | 23 | empty |
| 2 | 85 | 0.35 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2105 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5F6F · S. aureus MepR G34R Mutant · 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 Q5Y812
- Elsewhere: RCSB PDB 5F6F · PDBe 5F6F · UniProt Q5Y812
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