Research workbench
Structural and biochemical characterization of the hypothetical protein SAV2348 from staphylococcus aureus in complex with CoA.
Analyse Structural and biochemical characterization of the hypothetical protein SAV2348… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EO2
- Type
- protein
- Length
- 878 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioesterase
- UniProt
- A0A0H3JRH2
- Ligands
- COA
- Pockets
- 10 · best druggability 0.73
Structure
x-ray diffraction · 5 distinct chains · 24% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioesterase | protein | 133 | 23% helix, 35% strand | A0A0H3JRH2 |
| B | Thioesterase | protein | 154 | 26% helix, 37% strand | A0A0H3JRH2 |
| C, F | Thioesterase | protein | 158 | 25% helix, 37% strand | A0A0H3JRH2 |
| D | Thioesterase | protein | 120 | 21% helix, 34% strand | A0A0H3JRH2 |
| E | Thioesterase | protein | 155 | 25% helix, 37% strand | A0A0H3JRH2 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 6 copies · chains A, D, B, C, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.73 | 0.87 | 44 | empty |
| 2 | 195 | 0.73 | 0.89 | 40 | empty |
| 3 | 598 | 0.73 | 0.80 | 71 | COA |
| 4 | 197 | 0.72 | 0.88 | 42 | empty |
| 5 | 149 | 0.68 | 0.88 | 25 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1741 Ų buried · 33 hydrogen bonds · protein-protein
- E–F · 1730 Ų buried · 31 hydrogen bonds · protein-protein
- A–D · 1561 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 635 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 492 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5EO2 · Structural and biochemical characterization of the hypothetical protein SAV2348 from… · 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 A0A0H3JRH2
- Elsewhere: RCSB PDB 5EO2 · PDBe 5EO2 · UniProt A0A0H3JRH2
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