MolNFT v1 · #118406 · protein
X-ray crystal structure of a thiolase from escherichia COLI at 1.8 a resolution
5F0V · Acetyl-CoA acetyltransferase: “X-ray crystal structure of a thiolase from escherichia COLI at 1.8 a resolution”. X-ray diffraction, 19 pockets (best druggability 0.63). MolNFT v1 #118406 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5F0V
- Type
- protein
- Length
- 1,579 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
- P76461
- Pockets
- 19 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 395 | 39% helix, 24% strand | P76461 |
| B | Acetyl-CoA acetyltransferase (EC 2.3.1.9) | protein | 394 | 40% helix, 24% strand | P76461 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 44 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.63 | 0.86 | 23 | EDO |
| 2 | 158 | 0.61 | 0.84 | 24 | EDO |
| 3 | 171 | 0.60 | 0.83 | 27 | EDO |
| 4 | 170 | 0.59 | 0.82 | 25 | EDO |
| 5 | 136 | 0.57 | 0.83 | 28 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2662 Ų buried · 62 hydrogen bonds · protein-protein
- C–D · 2639 Ų buried · 62 hydrogen bonds · protein-protein
- A–D · 708 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 698 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 317 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (methylation).
Compared structures
- 5F0V · X-ray crystal structure of a thiolase from Escherichia coli at 1.8 A resolution · the same entry in another collection · chain D against D, TM-score 1.00
- P76461 · AlphaFold monomer V2.0 prediction for acetyl-CoA acetyltransferase (P76461) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P76461
- Elsewhere: RCSB PDB 5F0V · PDBe 5F0V · UniProt P76461
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