Research workbench
Serine protease splb from staphylococcus aureus at 1.8A resolution
Analyse Serine protease splb from staphylococcus aureus at 1.8A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VID
- Type
- protein
- Length
- 399 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease splb
- UniProt
- Q9KH50
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine protease splb | protein | 199 | 12% helix, 41% strand | Q9KH50 |
| B | Serine protease splb | protein | 200 | 11% helix, 41% strand | Q9KH50 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 377 | 0.65 | 0.79 | 45 | empty |
| 2 | 124 | 0.47 | 0.79 | 22 | empty |
| 3 | 78 | 0.41 | 0.79 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 504 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2VID · Serine protease SplB from Staphylococcus aureus at 1.8A resolution · 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 Q9KH50
- Elsewhere: RCSB PDB 2VID · PDBe 2VID · UniProt Q9KH50
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.