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6T8R

3C-like protease from Southampton virus complexed with FMOPL000605a.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
B0004197molecular_functioncysteine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue GVY A 201
ChainResidue
AVAL20
AGLY70
AMET71
AGLN172

site_idAC2
Number of Residues4
Detailsbinding site for residue PO4 A 202
ChainResidue
ACYS77
AILE104
AGLN117
ADMS205

site_idAC3
Number of Residues3
Detailsbinding site for residue PO4 A 203
ChainResidue
ALEU122
BLEU122
AARG100

site_idAC4
Number of Residues3
Detailsbinding site for residue DMS A 204
ChainResidue
AARG89
AGLU93
ALEU95

site_idAC5
Number of Residues4
Detailsbinding site for residue DMS A 205
ChainResidue
AGLU75
AGLY76
APRO78
APO4202

site_idAC6
Number of Residues5
Detailsbinding site for residue GVY B 201
ChainResidue
BVAL20
BVAL24
BARG59
BMET71
BGLN172

site_idAC7
Number of Residues5
Detailsbinding site for residue PO4 B 202
ChainResidue
BCYS77
BILE104
BGLN117
BDMS204
BHOH335

site_idAC8
Number of Residues4
Detailsbinding site for residue DMS B 203
ChainResidue
BTHR10
BTRP19
BPHE40
BARG65

site_idAC9
Number of Residues3
Detailsbinding site for residue DMS B 204
ChainResidue
BGLU75
BGLY76
BPO4202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: For 3CLpro activity => ECO:0000255|PROSITE-ProRule:PRU00870
ChainResidueDetails
BHIS30
BGLU54
BCYS139

226262

PDB entries from 2024-10-16

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