MolNFT v1 · #110059 · protein

Crystal structure of reduced form of thiolase from clostridium acetobutylicum

4XL3 · Acetyl-CoA acetyltransferase: “Crystal structure of reduced form of thiolase from clostridium acetobutylicum”. X-ray diffraction, 6 pockets (best druggability 0.55). MolNFT v1 #110059 on GenesisL1: 3D structure, binding sites and…

PDB: 4XL3
Type: protein
Length: 786 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Acetyl-CoA acetyltransferase
EC: 2.1.3.9
UniProt: F0K5D8
Pockets: 6 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Acetyl-CoA acetyltransferase (EC 2.1.3.9)	protein	393	39% helix, 24% strand	F0K5D8

Ligands and binding sites

GOL · Glycerol · additive · 6 copies · chains A, B

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

Pockets

6 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	195	0.55	0.79	35	GOL
2	136	0.54	0.81	32	GOL
3	172	0.49	0.77	35	empty
4	147	0.49	0.78	34	empty
5	151	0.48	0.78	23	GOL

Interfaces

1 interface between chains.

A–B · 2732 Å² buried · 67 hydrogen bonds · protein-protein

Compared structures

4XL3 · Crystal structure of reduced form of thiolase from Clostridium acetobutylicum · 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 F0K5D8
Elsewhere: RCSB PDB 4XL3 · PDBe 4XL3 · UniProt F0K5D8

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