MolNFT v1 · #39978 · protein
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of potassium and chloride for its structure and function
2IBU · Acetyl-CoA acetyltransferase: “Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of…”. X-ray diffraction, 2 ligands (COA, CL), 12 pockets (best druggability 0.56). MolNFT v1…
- PDB
- 2IBU
- Type
- protein
- Length
- 1,568 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
- P24752
- Ligands
- COA, CL
- Pockets
- 12 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 391 | 39% helix, 25% strand | P24752 |
| C, D | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 393 | 39% helix, 25% strand | P24752 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 4 copies · chains A, B, D, C
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 181 | 0.56 | 0.80 | 32 | COA |
| 2 | 177 | 0.56 | 0.80 | 33 | COA |
| 3 | 167 | 0.56 | 0.80 | 33 | COA |
| 4 | 167 | 0.55 | 0.80 | 34 | COA |
| 5 | 211 | 0.50 | 0.76 | 37 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2773 Ų buried · 58 hydrogen bonds · protein-protein
- A–B · 2706 Ų buried · 55 hydrogen bonds · protein-protein
- B–D · 618 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 608 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 333 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (oxidation).
Compared structures
- 2IBU · Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase… · the same entry in another collection · chain A against A, TM-score 1.00
- P24752 · AlphaFold monomer V2.0 prediction for acetyl-CoA acetyltransferase, mitochondrial (P24752) · a predicted model of the same protein · chain C 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 P24752
- Elsewhere: RCSB PDB 2IBU · PDBe 2IBU · UniProt P24752
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