MolNFT v1 · #117714 · protein
The structural and biochemical characterization of acyl-CoA hydrolase mutant ASP43ALA from staphylococcus aureus
5EGK · Acyl CoA hydrolase: “The structural and biochemical characterization of acyl-CoA hydrolase mutant ASP43ALA from staphylococcus…”. X-ray diffraction, 20 pockets (best druggability 0.82). MolNFT v1 #117714 on GenesisL1: 3D structure…
- PDB
- 5EGK
- Type
- protein
- Length
- 991 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl CoA hydrolase
- UniProt
- A0A0H3K033
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 33% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl CoA hydrolase | protein | 166 | 34% helix, 40% strand | A0A0H3K033 |
| B, F | Acyl CoA hydrolase | protein | 164 | 34% helix, 41% strand | A0A0H3K033 |
| C | Acyl CoA hydrolase | protein | 163 | 32% helix, 41% strand | A0A0H3K033 |
| D, E | Acyl CoA hydrolase | protein | 167 | 34% helix, 40% strand | A0A0H3K033 |
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 | 1028 | 0.82 | 0.83 | 80 | empty |
| 2 | 298 | 0.78 | 0.90 | 40 | empty |
| 3 | 136 | 0.74 | 0.93 | 36 | empty |
| 4 | 234 | 0.70 | 0.86 | 30 | empty |
| 5 | 283 | 0.68 | 0.83 | 42 | empty |
Interfaces
12 interfaces between chains.
- D–F · 1849 Ų buried · 18 hydrogen bonds · protein-protein
- B–E · 1843 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 1759 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 984 Ų buried · 12 hydrogen bonds · protein-protein
- A–E · 978 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 5EGK · The structural and biochemical characterization of acyl-coa hydrolase mutant Asp43Ala… · 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 A0A0H3K033
- Elsewhere: RCSB PDB 5EGK · PDBe 5EGK · UniProt A0A0H3K033
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.