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Crystal structure of the main protease (3CLPRO/MPRO) of SARS-cov-2 at 1.65A resolution (spacegroup P2(1)).

Analyse Crystal structure of the main protease (3CLPRO/MPRO) of SARS-cov-2 at 1.65A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ALI
Type: protein
Length: 611 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3C-like proteinase
EC: 3.4.22.69
UniProt: P0DTD1
Pockets: 6 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 26% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3C-like proteinase (EC 3.4.22.69)	protein	306	26% helix, 29% strand	P0DTD1
B	3C-like proteinase (EC 3.4.22.69)	protein	305	26% helix, 29% strand	P0DTD1

Pockets

6 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	981	0.77	0.79	81	empty
2	350	0.58	0.76	47	empty
3	230	0.49	0.75	26	empty
4	194	0.49	0.76	25	empty
5	181	0.46	0.75	31	empty

Interfaces

1 interface between chains.

A–B · 1631 Å² buried · 43 hydrogen bonds · protein-protein

Compared structures

7ALI · Crystal structure of the main protease (3CLpro/Mpro) of SARS-CoV-2 at 1.65A resolution… · the same entry in another collection · chain A against A, TM-score 1.00

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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 7ALI · PDBe 7ALI · UniProt P0DTD1

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