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Crystal structure of SARS-cov-2 mpro at 2.0 a resolution -9

Analyse Crystal structure of SARS-cov-2 mpro at 2.0 a resolution -9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VK2
Type
protein
Length
306 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
3C-like proteinase
EC
3.4.22.69
UniProt
P0DTC1
Pockets
3 · best druggability 0.52

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A3C-like proteinase (EC 3.4.22.69)protein30625% helix, 28% strandP0DTC1

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1720.520.8518empty
21560.470.7720empty
31470.420.7526empty

Compared structures

  • 7VK2 · Crystal Structure of SARS-CoV-2 Mpro at 2.0 A resolution -9 · the same entry in another collection · chain A against A, TM-score 1.00

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