Research workbench
Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)
Analyse Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FO5
- Type
- protein
- Length
- 472 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Homo sapiens
- Molecule
- Thioesterase, adipose associated, isoform BFIT2
- UniProt
- Q52LP1
- Ligands
- TCE, CL
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · resolution 2 · 2 distinct chains · 33% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioesterase, adipose associated, isoform BFIT2 | protein | 239 | 33% helix, 33% strand | Q52LP1 |
| B | Thioesterase, adipose associated, isoform BFIT2 | protein | 233 | 33% helix, 34% strand | Q52LP1 |
Ligands and binding sites
- TCE · 3,3',3''-phosphanetriyltripropanoic acid · ligand · chains A
- CL · Chloride ion · ion · chains A, B
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 500 | 0.83 | 0.89 | 73 | 1PE |
| 2 | 189 | 0.82 | 0.96 | 30 | 1PE |
| 3 | 90 | 0.48 | 0.82 | 19 | empty |
| 4 | 183 | 0.46 | 0.75 | 28 | CL |
| 5 | 63 | 0.46 | 0.83 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 963 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 3FO5 · Human start domain of acyl-coenzyme a thioesterase 11 (ACOT11) · the same entry in another collection · 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 Q52LP1
- Elsewhere: RCSB PDB 3FO5 · PDBe 3FO5 · UniProt Q52LP1
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