Research workbench
Crystal structure of staphylococcus aureus lipoprotein, htsa
Analyse Crystal structure of staphylococcus aureus lipoprotein, htsa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EIW
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Htsa protein
- UniProt
- Q99S89
- Ligands
- CL
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Htsa protein | protein | 292 | 45% helix, 20% strand | Q99S89 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.49 | 0.79 | 21 | CL |
| 2 | 77 | 0.31 | 0.74 | 15 | empty |
Compared structures
- 3EIW · Crystal structure of Staphylococcus aureus lipoprotein, HtsA · 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 Q99S89
- Elsewhere: RCSB PDB 3EIW · PDBe 3EIW · UniProt Q99S89
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