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2ZU3

Complex structure of CVB3 3C protease with TG-0204998

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ZU3 A 501
ChainResidue
AHIS40
ACYS147
AHIS161
AVAL162
AGLY163
AGLY164
AASN165
AHOH317
AHOH389
AHOH402
AGLU71
AASN126
ALEU127
AGLY128
ATHR142
AARG143
AALA144
AGLY145

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For protease 3C activity => ECO:0000255|PROSITE-ProRule:PRU01222
ChainResidueDetails
AHIS40
AGLU71

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: For protease 3C activity => ECO:0000269|PubMed:33691586
ChainResidueDetails
ACYS147

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by protease 3C => ECO:0000250|UniProtKB:P03301
ChainResidueDetails
AGLN183

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1cqq
ChainResidueDetails
AGLY145
AHIS40
AGLU71
ACYS147

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PDB entries from 2024-11-06

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