Research workbench
Human mitochondrial acetoacetyl-CoA thiolase
Analyse Human mitochondrial acetoacetyl-CoA thiolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F2S
- Type
- protein
- Length
- 1,545 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA acetyltransferase, mitochondrial
- EC
- 2.3.1.9
- UniProt
- P24752
- Ligands
- COA, CL
- Pockets
- 14 · best druggability 0.64
Structure
x-ray diffraction · 4 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) | protein | 389 | 38% helix, 22% strand | P24752 |
| B | Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) | protein | 386 | 39% helix, 23% strand | P24752 |
| C | Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) | protein | 388 | 39% helix, 23% strand | P24752 |
| D | Acetyl-CoA acetyltransferase, mitochondrial (EC 2.3.1.9) | protein | 382 | 40% helix, 23% strand | P24752 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 3 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 449 | 0.64 | 0.77 | 61 | empty |
| 2 | 297 | 0.56 | 0.76 | 46 | empty |
| 3 | 150 | 0.54 | 0.80 | 28 | COA |
| 4 | 123 | 0.52 | 0.81 | 24 | empty |
| 5 | 109 | 0.52 | 0.81 | 22 | empty |
Interfaces
5 interfaces between chains.
- B–C · 2506 Ų buried · 49 hydrogen bonds · protein-protein
- A–D · 2502 Ų buried · 49 hydrogen bonds · protein-protein
- A–B · 873 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 278 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 137 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 modified (acetylation).
Compared structures
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 2F2S · PDBe 2F2S · UniProt P24752
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