Research workbench

Crystal structure of rat choline acetyltransferase

Analyse Crystal structure of rat choline acetyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q6X
Type: protein
Length: 1,200 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Choline O-acetyltransferase
EC: 2.3.1.6
UniProt: P32738
Ligands: NA
Pockets: 18 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Choline O-acetyltransferase (EC 2.3.1.6)	protein	600	46% helix, 15% strand	P32738

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

18 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	893	0.78	0.81	98	empty
2	766	0.77	0.81	78	empty
3	209	0.52	0.77	33	empty
4	174	0.49	0.77	34	empty
5	152	0.46	0.77	24	empty

Compared structures

1Q6X · Crystal structure of rat choline acetyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
P32738 · AlphaFold monomer V2.0 prediction for choline O-acetyltransferase (P32738) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P32738
Elsewhere: RCSB PDB 1Q6X · PDBe 1Q6X · UniProt P32738

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.