Research workbench
Crystal structure of thiolase mutation (V77Q,N153Y,A286K) from clostridium acetobutylicum
Analyse Crystal structure of thiolase mutation (V77Q,N153Y,A286K) from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WYR
- 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
- P45359
- Pockets
- 6 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 392 | 40% helix, 23% strand | P45359 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 131 | 0.53 | 0.81 | 29 | PEG |
| 2 | 129 | 0.53 | 0.81 | 30 | PEG |
| 3 | 187 | 0.51 | 0.77 | 35 | empty |
| 4 | 142 | 0.49 | 0.79 | 26 | empty |
| 5 | 179 | 0.48 | 0.76 | 32 | PEG |
Interfaces
1 interface between chains.
- A–B · 2774 Ų buried · 62 hydrogen bonds · protein-protein
Compared structures
- 4WYR · Crystal structure of thiolase mutation (V77Q,N153Y,A286K) from Clostridium acetobutylicum · the same entry in another collection · chain A against A, TM-score 1.00
- P45359 · AlphaFold monomer V2.0 prediction for acetyl-CoA acetyltransferase (P45359) · 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 P45359
- Elsewhere: RCSB PDB 4WYR · PDBe 4WYR · UniProt P45359
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