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6L0T

Crystal structure of senecavirus A 3C protease

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
B0004197molecular_functioncysteine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For protease 3C activity and deubiquitinase activity => ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:30408499
ChainResidueDetails
AHIS48
ACYS160
BHIS48
BCYS160

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: For protease 3C activity => ECO:0000255|PROSITE-ProRule:PRU01222
ChainResidueDetails
AASP84
BASP84

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by protease 3C => ECO:0000269|PubMed:35727031, ECO:0000305|PubMed:18420805
ChainResidueDetails
AGLN211
BGLN211

223790

PDB entries from 2024-08-14

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