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Acetyl-CoA acetyltransferase from bacillus cereus atcc 14579

Analyse Acetyl-CoA acetyltransferase from bacillus cereus atcc 14579 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CW5
Type: protein
Length: 786 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: Q814S6
Ligands: COA
Pockets: 5 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acetyl-CoA acetyltransferase (EC 2.3.1.9)	protein	392	40% helix, 22% strand	Q814S6
B	Acetyl-CoA acetyltransferase (EC 2.3.1.9)	protein	394	39% helix, 22% strand	Q814S6

Ligands and binding sites

COA · Coenzyme A · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	261	0.67	0.83	44	COA
2	237	0.64	0.82	40	COA
3	146	0.51	0.80	33	empty
4	156	0.49	0.78	34	empty
5	62	0.36	0.79	20	empty

Interfaces

1 interface between chains.

A–B · 2823 Å² buried · 65 hydrogen bonds · protein-protein

Compared structures

7CW5 · Acetyl-CoA acetyltransferase from Bacillus cereus ATCC 14579 · 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 Q814S6
Elsewhere: RCSB PDB 7CW5 · PDBe 7CW5 · UniProt Q814S6

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