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1WOF

Crystal Structure Of SARS-CoV Mpro in Complex with an Inhibitor N1

Functional Information from GO Data
ChainGOidnamespacecontents
A0008233molecular_functionpeptidase activity
A0019082biological_processviral protein processing
B0008233molecular_functionpeptidase activity
B0019082biological_processviral protein processing
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE I12 A 1145
ChainResidue
ATHR25
AHIS163
AHIS164
AMET165
AGLU166
AHIS172
AASP187
AARG188
AGLN189
ATHR190
AALA191
ATHR26
AGLN192
AHOH1257
AHOH1258
AHIS41
AMET49
APHE140
AASN142
AGLY143
ASER144
ACYS145

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE I12 B 2145
ChainResidue
BTHR26
BHIS41
BPHE140
BASN142
BGLY143
BSER144
BCYS145
BHIS163
BHIS164
BMET165
BGLU166
BPRO168
BHIS172
BASP187
BGLN189
BTHR190
BALA191
BHOH2259

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For 3CL-PRO activity => ECO:0000255|PROSITE-ProRule:PRU00772
ChainResidueDetails
AHIS41
ACYS145
BHIS41
BCYS145

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by 3CL-PRO => ECO:0000269|PubMed:14561748
ChainResidueDetails
AGLN306
BGLN306

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bx4
ChainResidueDetails
ACYS145
AHIS41

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2bx4
ChainResidueDetails
BCYS145
BHIS41

site_idMCSA1
Number of Residues3
DetailsM-CSA 830
ChainResidueDetails
AHIS41proton acceptor, proton donor
AGLY143electrostatic stabiliser
ACYS145electrostatic stabiliser

site_idMCSA2
Number of Residues3
DetailsM-CSA 830
ChainResidueDetails
BHIS41proton acceptor, proton donor
BGLY143electrostatic stabiliser
BCYS145electrostatic stabiliser

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PDB entries from 2025-07-02

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