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Crystal structure of ACAT2 thiolase from ascaris suum

Analyse Crystal structure of ACAT2 thiolase from ascaris suum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BJ9
Type: protein
Length: 770 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA acetyltransferase a
UniProt: F1KYX0
Ligands: K
Pockets: 4 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acetyl-CoA acetyltransferase a	protein	385	39% helix, 23% strand	F1KYX0

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains A, B

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	274	0.57	0.77	32	empty
2	114	0.51	0.80	21	empty
3	103	0.46	0.79	20	empty
4	52	0.36	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 217 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6BJ9 · Crystal structure of Acat2 thiolase from Ascaris suum · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt F1KYX0
Elsewhere: RCSB PDB 6BJ9 · PDBe 6BJ9 · UniProt F1KYX0

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