MolNFT v1 · #22523 · protein
Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA
1T7Q: “Crystal structure of the F565A mutant of murine carnitine acetyltransferase in complex with carnitine and CoA”. X-ray diffraction, 2 ligands (COA, 152), 11 pockets (best druggability 0.77). MolNFT v1 #22523 on GenesisL1: 3D…
- 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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