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Structure-based drug design and structural biology study of novel nonpeptide inhibitors of SARS-cov main protease

Analyse Structure-based drug design and structural biology study of novel nonpeptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GZ8
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Replicase polyprotein 1AB
EC: 3.4.22.-
UniProt: P59641
Ligands: F3F
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Replicase polyprotein 1AB (EC 3.4.22.-)	protein	306	25% helix, 29% strand	P59641

Ligands and binding sites

F3F · S-[5-(trifluoromethyl)-4H-1,2,4-triazol-3-yl] 5-(phenylethynyl)furan-2-carbothioate · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	226	0.52	0.77	27	F3F
2	119	0.40	0.75	25	empty

Compared structures

2GZ8 · Structure-Based Drug Design and Structural Biology Study of Novel Nonpeptide Inhibitors… · 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 P59641
Elsewhere: RCSB PDB 2GZ8 · PDBe 2GZ8 · UniProt P59641

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