Research workbench

Crystal structure of SARS-cov 3CLPRO in complex with the non-covalent inhibitor wu-04

Analyse Crystal structure of SARS-cov 3CLPRO in complex with the non-covalent inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7END
Type: protein
Length: 306 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Replicase polyprotein 1A
EC: 3.4.19.12, 3.4.22.-, 3.4.22.69
UniProt: P0C6U8
Ligands: J7R
Pockets: 2 · best druggability 0.49

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Replicase polyprotein 1A (EC 3.4.19.12, 3.4.22.-, 3.4.22.69)	protein	306	25% helix, 29% strand	P0C6U8

Ligands and binding sites

J7R · ~{N}-[(1~{S},2~{R})-2-[[4-bromanyl-2-(methylcarbamoyl)-6-nitro-phenyl]amino]cyclohexyl]isoquinoline-4-carboxamide · 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	213	0.49	0.76	26	J7R
2	137	0.41	0.74	21	empty

Compared structures

7END · Crystal structure of SARS-CoV 3CLpro in complex with the non-covalent inhibitor WU-04 · 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 P0C6U8
Elsewhere: RCSB PDB 7END · PDBe 7END · UniProt P0C6U8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.