MolNFT v1 · #16013 · protein

Structure of human carnitine acetyltransferase: molecular basis for fatty acyl transfer

1NM8 · Carnitine O-acetyltransferase: “Structure of human carnitine acetyltransferase: molecular basis for fatty acyl transfer”. X-ray diffraction, 8 pockets (best druggability 0.77). MolNFT v1 #16013 on GenesisL1: 3D structure, binding…

PDB: 1NM8
Type: protein
Length: 591 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carnitine O-acetyltransferase
EC: 2.3.1.7
UniProt: P43155
Pockets: 8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carnitine O-acetyltransferase (EC 2.3.1.7)	protein	591	45% helix, 16% strand	P43155

Pockets

8 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	853	0.77	0.80	74	empty
2	84	0.61	0.89	19	empty
3	131	0.47	0.78	19	empty
4	76	0.44	0.81	18	empty
5	88	0.42	0.79	21	empty

Compared structures

1NM8 · Structure of Human Carnitine Acetyltransferase: Molecular Basis for Fatty Acyl Transfer · the same entry in another collection · chain A against A, TM-score 1.00
P43155 · AlphaFold monomer V2.0 prediction for carnitine O-acetyltransferase (P43155) · a predicted model of the same protein · chain A 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 P43155
Elsewhere: RCSB PDB 1NM8 · PDBe 1NM8 · UniProt P43155

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