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2D2D

Crystal Structure Of SARS-CoV Mpro in Complex with an Inhibitor I2

Replaces:  1WNQ
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 Residues19
DetailsBINDING SITE FOR RESIDUE ENB A 307
ChainResidue
ATHR26
AHIS164
AMET165
AGLU166
APRO168
AHIS172
AGLN189
ATHR190
AALA191
AGLN192
AHOH338
ALEU27
AHIS41
AMET49
APHE140
ALEU141
AASN142
ACYS145
AHIS163

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ENB B 1145
ChainResidue
BTHR26
BLEU27
BHIS41
BMET49
BPHE140
BLEU141
BASN142
BGLY143
BSER144
BCYS145
BHIS163
BHIS164
BMET165
BGLU166
BPRO168
BHIS172
BGLN189
BTHR190
BALA191
BGLN192
BHOH1167
BHOH1206

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

224004

PDB entries from 2024-08-21

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