Research workbench
Kshv protease
Analyse Kshv protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FL1
- Type
- protein
- Length
- 399 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease
- UniProt
- O36607
- Ligands
- K
- Pockets
- 5 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease | protein | 192 | 34% helix, 23% strand | O36607 |
| B | Protease | protein | 207 | 33% helix, 25% strand | O36607 |
Ligands and binding sites
- K · Potassium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.44 | 0.82 | 16 | empty |
| 2 | 111 | 0.43 | 0.77 | 20 | empty |
| 3 | 64 | 0.38 | 0.79 | 15 | empty |
| 4 | 53 | 0.28 | 0.75 | 19 | empty |
| 5 | 51 | 0.26 | 0.73 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 1262 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1FL1 · Kshv protease · 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 O36607
- Elsewhere: RCSB PDB 1FL1 · PDBe 1FL1 · UniProt O36607
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