MolNFT v1 · #102028 · protein
Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha H16
4O9C · Acetyl-CoA acetyltransferase: “Crystal structure of beta-ketothiolase (phaa) from ralstonia eutropha H16”. X-ray diffraction, 1 ligand (COA), 20 pockets (best druggability 0.64). MolNFT v1 #102028 on GenesisL1: 3D structure, binding…
- PDB
- 4O9C
- Type
- protein
- Length
- 3,144 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyl-CoA acetyltransferase
- EC
- 2.3.1.9
- UniProt
- P14611
- Ligands
- COA
- Pockets
- 20 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 393 | 38% helix, 24% strand | P14611 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains C, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 640 | 0.64 | 0.74 | 66 | empty |
| 2 | 133 | 0.61 | 0.85 | 28 | empty |
| 3 | 205 | 0.60 | 0.81 | 36 | empty |
| 4 | 180 | 0.60 | 0.82 | 34 | empty |
| 5 | 151 | 0.60 | 0.83 | 30 | empty |
Interfaces
16 interfaces between chains.
- E–F · 2705 Ų buried · 61 hydrogen bonds · protein-protein
- A–B · 2672 Ų buried · 59 hydrogen bonds · protein-protein
- C–D · 2659 Ų buried · 59 hydrogen bonds · protein-protein
- G–H · 2657 Ų buried · 60 hydrogen bonds · protein-protein
- A–E · 747 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 4O9C · Crystal structure of Beta-ketothiolase (PhaA) from Ralstonia eutropha H16 · the same entry in another collection · chain H against H, TM-score 1.00
- P14611 · AlphaFold monomer V2.0 prediction for acetyl-CoA acetyltransferase (P14611) · 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 P14611
- Elsewhere: RCSB PDB 4O9C · PDBe 4O9C · UniProt P14611
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