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Crystal structure of a chimeric murine norovirus NS6 protease (inactive C139A mutant) in which the P4-P4 prime residues of the cleavage junction in the extended C-terminus have been replaced by the corresponding residues from the NS2-3 junction.

Analyse Crystal structure of a chimeric murine norovirus NS6 protease (inactive C139A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4X2Y
Type
protein
Length
347 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NS6 PROTEASE,NS6 protease
UniProt
Q80J95
Pockets
1 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANS6 PROTEASE,NS6 proteaseprotein1723% helix, 48% strandQ80J95
BNS6 PROTEASE,NS6 proteaseprotein1755% helix, 49% strandQ80J95

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11310.660.8825empty

Interfaces

1 interface between chains.

  • A–B · 539 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 4X2Y · Crystal structure of a chimeric Murine Norovirus NS6 protease (inactive C139A mutant) in… · the same entry in another collection · chain A against A, TM-score 1.00

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