Research workbench
Crystal structure of S. aureus mepr in DNA-binding conformation
Analyse Crystal structure of S. aureus mepr in DNA-binding conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L9J
- Type
- protein
- Length
- 275 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mepr
- UniProt
- Q5Y812
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mepr | protein | 138 | 72% helix, 7% strand | Q5Y812 |
| B | Mepr | protein | 137 | 70% helix, 9% strand | Q5Y812 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.65 | 0.83 | 37 | empty |
| 2 | 221 | 0.58 | 0.79 | 23 | empty |
| 3 | 137 | 0.54 | 0.81 | 17 | empty |
| 4 | 75 | 0.33 | 0.75 | 9 | empty |
Interfaces
1 interface between chains.
- A–B · 2475 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 4L9J · Crystal structure of S. aureus MepR in DNA-binding conformation · 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 4L9J · PDBe 4L9J · UniProt Q5Y812
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