Research workbench
Crystal Structure of Apo-Hexameric Acyl-CoA Thioesterase
Analyse Crystal Structure of Apo-Hexameric Acyl-CoA Thioesterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SPS
- Type
- protein
- Length
- 933 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Bacillus halodurans
- Molecule
- Acyl-CoA hydrolase
- EC
- 3.1.2.-
- UniProt
- Q9KEQ1
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · resolution 2.9 · 2 distinct chains · 30% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | Acyl-CoA hydrolase (EC 3.1.2.-) | protein | 156 | 31% helix, 43% strand | Q9KEQ1 |
| C, D, F | Acyl-CoA hydrolase (EC 3.1.2.-) | protein | 155 | 30% helix, 42% strand | Q9KEQ1 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1093 | 0.83 | 0.84 | 71 | empty |
| 2 | 140 | 0.64 | 0.86 | 23 | empty |
| 3 | 148 | 0.62 | 0.85 | 34 | empty |
| 4 | 135 | 0.62 | 0.86 | 29 | empty |
| 5 | 129 | 0.62 | 0.86 | 24 | empty |
Interfaces
12 interfaces between chains.
- A–B · 1488 Ų buried · 24 hydrogen bonds · protein-protein
- C–E · 1362 Ų buried · 23 hydrogen bonds · protein-protein
- D–F · 1198 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 903 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 898 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3SPS · Crystal structure of apo-hexameric acyl-CoA thioesterase · 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 Q9KEQ1
- Elsewhere: RCSB PDB 3SPS · PDBe 3SPS · UniProt Q9KEQ1
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