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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMazF mRNA interferase (EC 3.1.-.-)protein11420% helix, 38% strandQ7A4G9
BMazF mRNA interferase (EC 3.1.-.-)protein11320% helix, 38% strandQ7A4G9

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1500.260.7415empty

Interfaces

1 interface between chains.

  • A–B · 1294 Ų buried · 30 hydrogen bonds · protein-protein

Compared structures

  • 4MZT · Mazf from S. aureus crystal form II, C2221, 2.3 a · the same entry in another collection · chain A against A, TM-score 1.00
  • Q7A4G9 · AlphaFold monomer V2.0 prediction for endoribonuclease mazf (Q7A4G9) · a predicted model of the same protein · chain B against A, TM-score 0.94

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