Research workbench
PURIFICATION,CRYSTALLIZATION and structural analysis of cytoplastic acetoacetyl-CoA thiolase from saccharomyces cerevisiae
Analyse PURIFICATION,CRYSTALLIZATION and structural analysis of cytoplastic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XYJ
- Type
- protein
- Length
- 792 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
- P41338
- Pockets
- 4 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 396 | 38% helix, 22% strand | P41338 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.62 | 0.80 | 39 | GOL |
| 2 | 221 | 0.59 | 0.80 | 41 | GOL |
| 3 | 69 | 0.34 | 0.76 | 17 | empty |
| 4 | 50 | 0.29 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- B–A · 306 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5XYJ · Purification,crystallization and structural analysis of cytoplastic acetoacetyl-CoA… · the same entry in another collection · chain B against B, TM-score 1.00
- P41338 · AlphaFold monomer V2.0 prediction for acetyl-CoA acetyltransferase (P41338) · a predicted model of the same protein · chain B 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 P41338
- Elsewhere: RCSB PDB 5XYJ · PDBe 5XYJ · UniProt P41338
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