Research workbench
Crystal structure of HI0827, a hexameric broad specificity acyl- coenzyme a thioesterase: the ASP44ALA mutant enzyme
Analyse Crystal structure of HI0827, a hexameric broad specificity acyl- coenzyme a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BJK
- Type
- protein
- Length
- 841 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-CoA thioester hydrolase HI0827
- EC
- 3.1.2.-
- UniProt
- P44886
- Pockets
- 13 · best druggability 0.83
Structure
x-ray diffraction · 5 distinct chains · 24% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Acyl-CoA thioester hydrolase HI0827 (EC 3.1.2.-) | protein | 140 | 24% helix, 41% strand | P44886 |
| B | Acyl-CoA thioester hydrolase HI0827 (EC 3.1.2.-) | protein | 142 | 24% helix, 40% strand | P44886 |
| C | Acyl-CoA thioester hydrolase HI0827 (EC 3.1.2.-) | protein | 142 | 23% helix, 40% strand | P44886 |
| D | Acyl-CoA thioester hydrolase HI0827 (EC 3.1.2.-) | protein | 139 | 25% helix, 41% strand | P44886 |
| F | Acyl-CoA thioester hydrolase HI0827 (EC 3.1.2.-) | protein | 138 | 25% helix, 40% strand | P44886 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 25 copies · chains A, D, B, E, C, F
- CIT · Citric acid · additive · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 834 | 0.83 | 0.85 | 73 | EDO |
| 2 | 232 | 0.74 | 0.89 | 35 | empty |
| 3 | 279 | 0.74 | 0.87 | 40 | empty |
| 4 | 224 | 0.73 | 0.88 | 35 | empty |
| 5 | 319 | 0.73 | 0.85 | 37 | empty |
Interfaces
12 interfaces between chains.
- B–E · 957 Ų buried · 12 hydrogen bonds · protein-protein
- C–F · 937 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 928 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 836 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 742 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 3BJK · Crystal structure of HI0827, a hexameric broad specificity acyl-coenzyme A thioesterase… · the same entry in another collection · chain F against F, TM-score 1.00
- P44886 · AlphaFold monomer V2.0 prediction for uncharacterized acyl-CoA thioester hydrolase… · a predicted model of the same protein · chain D 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 P44886
- Elsewhere: RCSB PDB 3BJK · PDBe 3BJK · UniProt P44886
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