Research workbench
Fmdv leader protease bound to substrate ISG15
Analyse Fmdv leader protease bound to substrate ISG15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FFA
- Type
- protein
- Length
- 233 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lbpro; Ubiquitin-like protein ISG15
- UniProt
- P03305, P05161
- Ligands
- AYE, SO4
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lbpro | protein | 156 | 29% helix, 28% strand | P03305 |
| B | Ubiquitin-like protein ISG15 | protein | 77 | 25% helix, 35% strand | P05161 |
Ligands and binding sites
- AYE · prop-2-en-1-amine · ligand · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 5 copies · chains A, B
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 | 249 | 0.71 | 0.86 | 35 | empty |
| 2 | 80 | 0.32 | 0.74 | 20 | GOL |
Interfaces
1 interface between chains.
- A–B · 675 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 P03305
- Every structure of UniProt P05161
- Elsewhere: RCSB PDB 6FFA · PDBe 6FFA · UniProt P03305 · UniProt P05161
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