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1CQQ

TYPE 2 RHINOVIRUS 3C PROTEASE WITH AG7088 INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE AG7 A 501
ChainResidue
APRO2
AASN130
ATHR142
ALYS143
AGLY145
ATYR146
ACYS147
AHIS161
AVAL162
AGLY163
AGLY164
AASN22
AASN165
APHE170
AHOH739
AHOH823
ALYS24
APHE25
AHIS40
AGLU71
ALEU126
ALEU127
ASER128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues178
DetailsDomain: {"description":"Peptidase C3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01222","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"For protease 3C activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01222","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 10500114, 2158990, 7515772, 20107288, 9060667
ChainResidueDetails
ACYS147
ACYS147
AHIS40
AGLU71
AGLY145

site_idMCSA1
Number of Residues4
DetailsM-CSA 477
ChainResidueDetails
AHIS40electrostatic stabiliser, proton shuttle (general acid/base)
AGLU71electrostatic stabiliser, modifies pKa
AGLY145electrostatic stabiliser
ACYS147electrostatic stabiliser

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PDB entries from 2025-10-22

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