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Truncated hemolysin a Q125A/Y134A from P. mirabilis at 1.8 ångströms resolution crystallized in a high salt condition

Analyse Truncated hemolysin a Q125A/Y134A from P. mirabilis at 1.8 ångströms resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5SZ8
Type
protein
Length
408 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemolysin
UniProt
P16466
Ligands
SO4
Pockets
1 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemolysinprotein2051% helix, 56% strandP16466
BHemolysinprotein2030% helix, 56% strandP16466

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1510.710.9818empty

Interfaces

1 interface between chains.

  • A–B · 748 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 5SZ8 · Truncated hemolysin A Q125A/Y134A from P. mirabilis at 1.8 Angstroms resolution… · the same entry in another collection · chain A against A, TM-score 1.00
  • P16466 · AlphaFold monomer V2.0 prediction for hemolysin (P16466) · a predicted model of the same protein · chain B against A, TM-score 0.99

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