Research workbench
Structure of V8 protease from staphylococcus aureus
Analyse Structure of V8 protease 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
- 2O8L
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- V8 protease
- EC
- 3.4.21.19
- UniProt
- Q99V45
- Ligands
- K
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V8 protease (EC 3.4.21.19) | protein | 216 | 10% helix, 42% strand | Q99V45 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q99V45
- Elsewhere: RCSB PDB 2O8L · PDBe 2O8L · UniProt Q99V45
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