Research workbench
Crystal structure of se-met derivative mepr F27L mutant from multidrug resistant S. aureus clinical isolate
Analyse Crystal structure of se-met derivative mepr F27L mutant from multidrug… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L9V
- Type
- protein
- Length
- 139 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mepr
- UniProt
- Q5Y812
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mepr | protein | 139 | 72% helix, 8% strand | Q5Y812 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.35 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 4L9V · Crystal structure of Se-Met derivative MepR F27L mutant from multidrug resistant S.… · 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 4L9V · PDBe 4L9V · UniProt Q5Y812
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