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2B0F

NMR Structure of the Human Rhinovirus 3C Protease (serotype 14) with covalently bound Ace-LEALFQ-ethylpropionate inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR CHAIN B OF ACE-LEALFQ-ETHYLPROPIONATE
ChainResidue
ALYS22
ALYS142
ATHR143
AGLY144
ACYS146
AHIS160
AVAL161
AGLY162
AGLY163
AASN164
APHE169
AHIS40
AGLU71
AILE124
AASN125
ALEU126
ASER127
ASER128
ATHR141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: For protease 3C activity => ECO:0000255|PROSITE-ProRule:PRU01222
ChainResidueDetails
AHIS40
AGLU71
ACYS146

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by protease 3C => ECO:0000250|UniProtKB:P03301
ChainResidueDetails
AGLN182

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1cqq
ChainResidueDetails
AHIS40
AGLU71
AGLY144
ACYS146

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PDB entries from 2024-07-24

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