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6T3G

3C-like protease from Southampton virus complexed with FMOPL000324a.

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 Residues2
Detailsbinding site for residue JOV A 201
ChainResidue
AGLY13
AHOH425

site_idAC2
Number of Residues5
Detailsbinding site for residue PO4 A 202
ChainResidue
AARG89
AGLU93
AASP131
BTHR4
BTRP6

site_idAC3
Number of Residues8
Detailsbinding site for residue PO4 A 203
ChainResidue
AILE135
APRO136
AALA160
ATHR161
AHOH304
AHOH316
AGLN110
ATHR134

site_idAC4
Number of Residues5
Detailsbinding site for residue PO4 A 204
ChainResidue
ACYS77
AGLY102
AGLN117
ADMS206
AHOH371

site_idAC5
Number of Residues4
Detailsbinding site for residue DMS A 205
ChainResidue
AVAL82
ALYS146
AHOH397
BMET130

site_idAC6
Number of Residues5
Detailsbinding site for residue DMS A 206
ChainResidue
AGLU75
AGLY76
ACYS77
APO4204
AHOH371

site_idAC7
Number of Residues2
Detailsbinding site for residue DMS A 207
ChainResidue
ASER7
AARG65

site_idAC8
Number of Residues3
Detailsbinding site for residue PO4 B 201
ChainResidue
BPRO66
BASP67
BLEU68

site_idAC9
Number of Residues3
Detailsbinding site for residue DMS B 202
ChainResidue
BCYS77
BGLY102
BHOH354

site_idAD1
Number of Residues4
Detailsbinding site for residue DMS B 203
ChainResidue
BTHR10
BTRP19
BPHE40
BARG65

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

219869

PDB entries from 2024-05-15

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