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Murine acyloxyacyl hydrolase (AOAH), S262A mutant

Analyse Murine acyloxyacyl hydrolase (AOAH), S262A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5W7D
Type
protein
Length
528 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.75
Source
Mus musculus
Molecule
Acyloxyacyl hydrolase
EC
3.1.1.77
UniProt
O35298
Ligands
PX8, MYR, NAG, CA
Pockets
4 · best druggability 0.82

Structure

x-ray diffraction · resolution 1.75 · 1 distinct chain · 47% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcyloxyacyl hydrolase (EC 3.1.1.77)protein52847% helix, 8% strandO35298

Ligands and binding sites

  • PX8 · 1,2-distearoyl-sn-glycero-3-phosphate · ligand · chains A
  • MYR · Myristic acid · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
  • CA · Calcium ion · metal · 3 copies · chains A
  • GOL · Glycerol · additive · chains 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110650.820.8282PX8, MYR
2640.730.9820empty
3530.380.8113empty
4920.360.7516empty

Modifications

Observed in the structure: 8 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

  • 5W7D · Murine acyloxyacyl hydrolase (aoah), S262A mutant · the same entry in another collection · chain A against A, TM-score 1.00
  • O35298 · AlphaFold monomer V2.0 prediction for acyloxyacyl hydrolase (O35298) · a predicted model of the same protein · chain A against A, TM-score 1.00

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