Research workbench
Novel crystal structure of dhna-CoA thioesterase from staphylococcus aureus
Analyse Novel crystal structure of dhna-CoA thioesterase from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FDG
- Type
- protein
- Length
- 608 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxybenzoyl-CoA thioesterase
- UniProt
- A0A166E508
- Pockets
- 9 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | 4-hydroxybenzoyl-CoA thioesterase | protein | 155 | 30% helix, 37% strand | A0A166E508 |
| B, D | 4-hydroxybenzoyl-CoA thioesterase | protein | 149 | 32% helix, 37% strand | A0A166E508 |
Pockets
9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 404 | 0.86 | 0.95 | 33 | empty |
| 2 | 192 | 0.78 | 0.92 | 42 | empty |
| 3 | 212 | 0.77 | 0.91 | 40 | empty |
| 4 | 89 | 0.77 | 0.98 | 25 | empty |
| 5 | 217 | 0.76 | 0.90 | 41 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1127 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1123 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 655 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 653 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 449 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6FDG · Novel crystal structure of DHNA-CoA Thioesterase from Staphylococcus aureus · 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 A0A166E508
- Elsewhere: RCSB PDB 6FDG · PDBe 6FDG · UniProt A0A166E508
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