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PURIFICATION,CRYSTALLIZATION and structural analysis of cytoplastic acetoacetyl-CoA thiolase from saccharomyces cerevisiae

Analyse PURIFICATION,CRYSTALLIZATION and structural analysis of cytoplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XZ5
Type
protein
Length
777 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acetyl-CoA acetyltransferase
EC
2.3.1.9
UniProt
P41338
Pockets
3 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcetyl-CoA acetyltransferase (EC 2.3.1.9)protein38139% helix, 22% strandP41338
BAcetyl-CoA acetyltransferase (EC 2.3.1.9)protein39637% helix, 22% strandP41338

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13080.580.7729empty
21230.550.8229empty
3680.300.7416empty

Interfaces

1 interface between chains.

  • A–B · 282 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 5XZ5 · Purification,crystallization and structural analysis of cytoplastic acetoacetyl-CoA… · the same entry in another collection · chain A against A, TM-score 1.00
  • P41338 · AlphaFold monomer V2.0 prediction for acetyl-CoA acetyltransferase (P41338) · a predicted model of the same protein · chain B against A, TM-score 1.00

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