Research workbench
Crystal structure of Staphylococcus aureus Lysophosphatidylglycerol phospholipase D
Analyse Crystal structure of Staphylococcus aureus Lysophosphatidylglycerol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8GHI
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Staphylococcus aureus
- Molecule
- Glycerophosphodiester phosphodiesterase
- EC
- 3.1.4.46
- UniProt
- A0A0D6HT57
- Ligands
- 2HP
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · resolution 2.4 · 1 distinct chain · 36% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycerophosphodiester phosphodiesterase (EC 3.1.4.46) | protein | 275 | 36% helix, 19% strand | A0A0D6HT57 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.52 | 0.78 | 24 | 2HP |
| 2 | 69 | 0.37 | 0.77 | 16 | empty |
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 A0A0D6HT57
- Elsewhere: RCSB PDB 8GHI · PDBe 8GHI · UniProt A0A0D6HT57
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