Joint X-RAY/NEUTRON structure of SARS-cov-2 main protease (3CL mpro) in complex with bbh-1

Structure

x-ray diffraction; neutron diffraction · 1 distinct chain · 25% helix, 28% strand (DSSP).

Ligands and binding sites

• I1W · (1R,2S,5S)-N-{(1S,2S)-1-(1,3-benzothiazol-2-yl)-1-hydroxy-3-[(3S)-2-oxo(1-~2~H)pyrrolidin-3-yl]propan-2-yl}-3-{N-[tert-butyl(~2~H)carbamoyl]-3-methyl-L-(N-~2~H)valyl}-6,6-dimethyl-3-azabicyclo[3.1.0]hexane-2-(~2~H)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, 2 with a druggability of 0.5 or more.

Modifications

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

Compared structures

• 7TDU · Joint X-ray/neutron structure of SARS-CoV-2 main protease (3CL Mpro) in complex with BBH-1 · 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 P0DTD1
• Elsewhere: RCSB PDB 7TDU · PDBe 7TDU · UniProt P0DTD1