MolNFT v1 · #19582 · protein
Structure of the fmdv leader protease
1QOL · Protease (nonstructural protein P20A): “Structure of the fmdv leader protease”. X-ray diffraction, 1 ligand (CL), 15 pockets (best druggability 0.76). MolNFT v1 #19582 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1QOL
- Type
- protein
- Length
- 1,356 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease (nonstructural protein P20A)
- UniProt
- P03305
- Ligands
- CL
- Pockets
- 15 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E, F | Protease (nonstructural protein P20A) | protein | 166 | 28% helix, 27% strand | P03305 |
| C, D, G, H | Protease (nonstructural protein P20A) | protein | 173 | 26% helix, 27% strand | P03305 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains B, C, A, D, E, G
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, F, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1126 | 0.76 | 0.78 | 96 | empty |
| 2 | 1099 | 0.75 | 0.77 | 105 | CL |
| 3 | 120 | 0.56 | 0.83 | 26 | empty |
| 4 | 109 | 0.53 | 0.82 | 22 | empty |
| 5 | 109 | 0.53 | 0.82 | 17 | empty |
Interfaces
10 interfaces between chains.
- B–D · 1594 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1586 Ų buried · 28 hydrogen bonds · protein-protein
- F–G · 1531 Ų buried · 28 hydrogen bonds · protein-protein
- E–H · 1479 Ų buried · 26 hydrogen bonds · protein-protein
- A–F · 632 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1QOL · Structure of the fmdv leader 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 P03305
- Elsewhere: RCSB PDB 1QOL · PDBe 1QOL · UniProt P03305
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.