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3C protease of enterovirus 68 complexed with michael receptor inhibitor 85

Analyse 3C protease of enterovirus 68 complexed with michael receptor inhibitor 85 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZVF
Type: protein
Length: 188 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C protease
EC: 3.4.22.28
UniProt: A1E4A3
Ligands: G85
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C protease (EC 3.4.22.28)	protein	188	11% helix, 50% strand	A1E4A3

Ligands and binding sites

G85 · N-[(benzyloxy)carbonyl]-O-tert-butyl-L-seryl-N-{(2R)-5-ethoxy-5-oxo-1-[(3S)-2-oxopyrrolidin-3-yl]pentan-2-yl}-L-phenylalaninamide · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	109	0.38	0.75	19	empty
2	56	0.28	0.74	19	G85

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

3ZVF · 3C protease of Enterovirus 68 complexed with Michael receptor inhibitor 85 · 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 A1E4A3
Elsewhere: RCSB PDB 3ZVF · PDBe 3ZVF · UniProt A1E4A3

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