Research workbench
MazF from S. aureus crystal form II, C2221, 2.3 A
Analyse MazF from S. aureus crystal form II, C2221, 2.3 A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MZT
- Type
- protein
- Length
- 227 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.303
- Source
- Staphylococcus aureus subsp. aureus
- Molecule
- MazF mRNA interferase
- EC
- 3.1.-.-
- UniProt
- Q7A4G9
- Pockets
- 1 · best druggability 0.26
Structure
x-ray diffraction · resolution 2.303 · 2 distinct chains · 20% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MazF mRNA interferase (EC 3.1.-.-) | protein | 114 | 20% helix, 38% strand | Q7A4G9 |
| B | MazF mRNA interferase (EC 3.1.-.-) | protein | 113 | 20% helix, 38% strand | Q7A4G9 |
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 | 50 | 0.26 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1294 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
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 Q7A4G9
- Elsewhere: RCSB PDB 4MZT · PDBe 4MZT · UniProt Q7A4G9
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