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Structure of SARS-cov main protease bound to potent broad-spectrum non-covalent inhibitor X77

Analyse Structure of SARS-cov main protease bound to potent broad-spectrum non-covalent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6W79
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Main protease
Ligands: X77
Pockets: 2 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Main protease	protein	306	24% helix, 29% strand	—

Ligands and binding sites

X77 · N-(4-tert-butylphenyl)-N-[(1R)-2-(cyclohexylamino)-2-oxo-1-(pyridin-3-yl)ethyl]-1H-imidazole-4-carboxamide · ligand · chains A
MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 2 copies · chains A
DMS · Dimethyl sulfoxide · additive · 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	225	0.50	0.75	30	X77
2	113	0.38	0.74	25	empty

Compared structures

6W79 · Structure of SARS-CoV main protease bound to potent broad-spectrum non-covalent inhibitor… · 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
Elsewhere: RCSB PDB 6W79 · PDBe 6W79

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