MolNFT v1 · #121559 · protein
The structural and biochemical characterization of acyl-CoA hydrolase mutant THR60ALA from staphylococcus aureus.
5HZ4 · Thioesterase: “The structural and biochemical characterization of acyl-CoA hydrolase mutant THR60ALA from staphylococcus…”. X-ray diffraction, 15 pockets (best druggability 0.83). MolNFT v1 #121559 on GenesisL1: 3D structure…
- PDB
- 5HZ4
- Type
- protein
- Length
- 966 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioesterase
- UniProt
- A0A0H3K033
- Pockets
- 15 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 33% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, F | Thioesterase | protein | 162 | 35% helix, 41% strand | A0A0H3K033 |
| D | Thioesterase | protein | 159 | 31% helix, 40% strand | A0A0H3K033 |
| E | Thioesterase | protein | 159 | 33% helix, 41% strand | A0A0H3K033 |
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 582 | 0.83 | 0.88 | 88 | empty |
| 2 | 214 | 0.73 | 0.88 | 37 | empty |
| 3 | 213 | 0.72 | 0.88 | 36 | empty |
| 4 | 554 | 0.71 | 0.80 | 59 | empty |
| 5 | 108 | 0.69 | 0.92 | 27 | empty |
Interfaces
12 interfaces between chains.
- D–F · 1772 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1745 Ų buried · 27 hydrogen bonds · protein-protein
- B–E · 1710 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 907 Ų buried · 11 hydrogen bonds · protein-protein
- B–F · 892 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5HZ4 · The structural and biochemical characterization of acyl-coa hydrolase mutant Thr60Ala… · the same entry in another collection · chain D against D, 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 5HZ4 · PDBe 5HZ4 · UniProt A0A0H3K033
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