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Toxin protein from Staphylococcus aureus

Analyse Toxin protein from Staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7EWI
Type
protein
Length
446 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.93
Source
Staphylococcus aureus
Molecule
Endoribonuclease MazF
UniProt
L7PFJ6
Ligands
PO4
Pockets
4 · best druggability 0.55

Structure

x-ray diffraction · resolution 1.93 · 3 distinct chains · 19% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C, DEndoribonuclease MazFprotein11120% helix, 34% strandL7PFJ6
BEndoribonuclease MazFprotein10920% helix, 35% strandL7PFJ6
AEndoribonuclease MazFprotein11517% helix, 33% strandL7PFJ6

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 4 copies · chains C, B, A, D
  • GOL · Glycerol · additive · chains C, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12160.550.7830empty
21130.380.7422empty
3630.340.7713empty
4640.320.7513GOL

Interfaces

3 interfaces between chains.

  • B–D · 1773 Ų buried · 35 hydrogen bonds · protein-protein
  • C–A · 1765 Ų buried · 34 hydrogen bonds · protein-protein
  • C–B · 309 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 7EWI · Toxin protein from staphylococcus aureus · the same entry in another collection · chain A against A, TM-score 1.00

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