MolNFT v1 · #15717 · protein
Crystal structure of carnitine acetyltransferase
1NDB: “Crystal structure of carnitine acetyltransferase”. X-ray diffraction, 11 pockets (best druggability 0.76). MolNFT v1 #15717 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NDB
- Type
- protein
- Length
- 1,192 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
- Pockets
- 11 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carnitine acetyltransferase (EC 2.3.1.7) | protein | 596 | 44% helix, 15% strand | P47934 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 883 | 0.76 | 0.79 | 82 | empty |
| 2 | 830 | 0.76 | 0.79 | 80 | empty |
| 3 | 172 | 0.59 | 0.82 | 37 | empty |
| 4 | 196 | 0.56 | 0.80 | 24 | empty |
| 5 | 150 | 0.51 | 0.79 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 26 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 40 modified (engineered).
Compared structures
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 1NDB · PDBe 1NDB · UniProt P47934
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