Research workbench
Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA
Analyse Crystal structure of the F565A mutant of murine carnitine acetyltransferase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T7Q
- Type
- protein
- Length
- 1,198 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carnitine acetyltransferase
- EC
- 2.3.1.7
- UniProt
- P47934
- Ligands
- COA, 152
- Pockets
- 11 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carnitine acetyltransferase (EC 2.3.1.7) | protein | 599 | 45% helix, 15% strand | P47934 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
- 152 · Carnitine · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 866 | 0.77 | 0.80 | 83 | COA, 152, EDO |
| 2 | 826 | 0.76 | 0.80 | 78 | COA, 152, EDO |
| 3 | 182 | 0.56 | 0.80 | 27 | empty |
| 4 | 183 | 0.55 | 0.79 | 28 | empty |
| 5 | 132 | 0.49 | 0.79 | 21 | empty |
Compared structures
- 1T7Q · Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- P47934 · AlphaFold monomer V2.0 prediction for carnitine O-acetyltransferase (P47934) · a predicted model of the same protein · 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 P47934
- Elsewhere: RCSB PDB 1T7Q · PDBe 1T7Q · UniProt P47934
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