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Abeta-bound human abad structure [also known as 3-hydroxyacyl-CoA dehydrogenase type II (type II hadh), endoplasmic reticulum- associated amyloid beta-peptide binding protein (erab)]

Analyse Abeta-bound human abad structure [also known as 3-hydroxyacyl-CoA dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SO8
Type
protein
Length
208 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
3-hydroxyacyl-CoA dehydrogenase type II
EC
1.1.1.35
UniProt
Q99714
Ligands
NA, CL
Pockets
2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A3-hydroxyacyl-CoA dehydrogenase type II (EC 1.1.1.35)protein20841% helix, 18% strandQ99714

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11250.400.7522empty
2760.380.7818empty

Compared structures

  • 1SO8 · Abeta-bound human ABAD structure [also known as 3-hydroxyacyl-CoA dehydrogenase type II… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q99714 · AlphaFold monomer V2.0 prediction for 3-hydroxyacyl-CoA dehydrogenase type-2 (Q99714) · a predicted model of the same protein · chain A against A, TM-score 0.90

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