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Structure of the SARS-cov-2 main protease in complex with inhibitor MPI22

Analyse Structure of the SARS-cov-2 main protease in complex with inhibitor MPI22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RVV
Type: protein
Length: 303 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like proteinase
UniProt: P0DTD1
Ligands: 7Y2
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C-like proteinase	protein	303	22% helix, 25% strand	P0DTD1

Ligands and binding sites

7Y2 · N-[(benzyloxy)carbonyl]-2-methyl-L-alanyl-N-{(2S)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-4-methyl-L-leucinamide · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	211	0.53	0.78	29	7Y2
2	209	0.51	0.76	30	empty

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

7RVV · Structure of the SARS-CoV-2 main protease in complex with inhibitor MPI22 · 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 7RVV · PDBe 7RVV · UniProt P0DTD1

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