MolNFT v1 · #143138 · protein
Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with CoA and potassium ions
6AQP · Acetyl-CoA acetyltransferase: “Aspergillus fumigatus cytosolic thiolase: acetylated enzyme in complex with CoA and potassium ions”. X-ray diffraction, 4 ligands (COA, ACO, K), 11 pockets (best druggability 0.57). MolNFT v1 #143138…
- PDB
- 6AQP
- Type
- protein
- Length
- 1,589 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA acetyltransferase
- EC
- 2.3.1.9
- UniProt
- Q4WCL5
- Ligands
- COA, ACO, K, CL
- Pockets
- 11 · best druggability 0.57
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 397 | 40% helix, 23% strand | Q4WCL5 |
| B | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 396 | 39% helix, 23% strand | Q4WCL5 |
| C | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 399 | 38% helix, 23% strand | Q4WCL5 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 3 copies · chains A, B, C, D
- ACO · Acetyl coenzyme *A · ligand · chains B, C
- K · Potassium ion · metal · 12 copies · chains A, B, C, D
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
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 | 239 | 0.57 | 0.78 | 32 | K, ACO |
| 2 | 190 | 0.57 | 0.80 | 27 | COA |
| 3 | 233 | 0.56 | 0.78 | 31 | COA, K |
| 4 | 186 | 0.54 | 0.78 | 34 | COA, K |
| 5 | 152 | 0.50 | 0.78 | 19 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2701 Ų buried · 48 hydrogen bonds · protein-protein
- A–B · 2684 Ų buried · 49 hydrogen bonds · protein-protein
- B–C · 814 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 798 Ų buried · 12 hydrogen bonds · protein-protein
- B–D · 388 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 2 covalent (acetylation, covalent ligand).
Compared structures
- 6AQP · Aspergillus fumigatus Cytosolic Thiolase: Acetylated enzyme in complex with CoA and… · 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 Q4WCL5
- Elsewhere: RCSB PDB 6AQP · PDBe 6AQP · UniProt Q4WCL5
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