Research workbench
Crystal structure of reduced form of thiolase from clostridium acetobutylicum
Analyse Crystal structure of reduced form of thiolase from clostridium acetobutylicum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N45
- Type
- protein
- Length
- 784 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA acetyltransferase
- EC
- 2.3.1.9
- UniProt
- F0K5D8
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 392 | 39% helix, 23% strand | F0K5D8 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 139 | 0.56 | 0.82 | 30 | empty |
| 2 | 136 | 0.56 | 0.82 | 29 | empty |
| 3 | 194 | 0.52 | 0.78 | 29 | empty |
| 4 | 184 | 0.50 | 0.77 | 37 | empty |
| 5 | 149 | 0.49 | 0.78 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 2734 Ų buried · 66 hydrogen bonds · protein-protein
Compared structures
- 4N45 · Crystal structure of reduced form of thiolase from Clostridium acetobutylicum · 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 F0K5D8
- Elsewhere: RCSB PDB 4N45 · PDBe 4N45 · UniProt F0K5D8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.