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Crystal structure of murine carnitine acetyltransferase in complex with carnitine and CoA

Analyse Crystal structure of murine carnitine acetyltransferase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2H3U
Type: protein
Length: 1,198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carnitine acetyltransferase
UniProt: Q3V1Y3
Ligands: COA, 152
Pockets: 12 · best druggability 0.76

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Carnitine acetyltransferase	protein	599	46% helix, 15% strand	Q3V1Y3

Ligands and binding sites

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

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	779	0.76	0.80	73	COA, 152
2	831	0.76	0.80	74	COA, 152
3	194	0.57	0.80	27	empty
4	192	0.54	0.79	24	empty
5	95	0.52	0.83	22	empty

Compared structures

2H3U · Crystal structure of murine carnitine acetyltransferase in complex with carnitine and CoA · 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 Q3V1Y3
Elsewhere: RCSB PDB 2H3U · PDBe 2H3U · UniProt Q3V1Y3

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