MolNFT v1 · #84278 · protein
Crystal structure of substrate-like, unprocessed N-terminal protease npro mutant S169P with sulphate
3ZFU: “Crystal structure of substrate-like, unprocessed N-terminal protease npro mutant S169P with sulphate”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.36). MolNFT v1 #84278 on GenesisL1: 3D structure, binding sites…
- PDB
- 3ZFU
- Type
- protein
- Length
- 150 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-terminal protease npro
- EC
- 3.4.22.-
- UniProt
- Q5L4B1
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-terminal protease npro (EC 3.4.22.-) | protein | 150 | 7% helix, 36% strand | Q5L4B1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 89 | 0.36 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 2 disulfide, 1 covalent (disulfide, additive adduct).
Compared structures
- 3ZFU · Crystal structure of substrate-like, unprocessed N-terminal protease Npro mutant S169P… · 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 Q5L4B1
- Elsewhere: RCSB PDB 3ZFU · PDBe 3ZFU · UniProt Q5L4B1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.