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3SND

Crystal structure of SARS coronavirus main protease complexed with Ac-ESTLQ-H (cocrystallization)

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 Residues9
DetailsBINDING SITE FOR RESIDUE MRD A 307
ChainResidue
APRO108
AGLY109
AILE200
ALEU202
AHIS246
AHOH322
AHOH366
AHOH454
AHOH534

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues610
DetailsDomain: {"description":"Peptidase C30","evidences":[{"source":"PROSITE-ProRule","id":"PRU00772","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"For 3CL-PRO activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00772","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
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 2025-12-03

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