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3EYD

Structure of HCV NS3-4A Protease with an Inhibitor Derived from a Boronic Acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0019087biological_processsymbiont-mediated transformation of host cell
C0006508biological_processproteolysis
C0008236molecular_functionserine-type peptidase activity
C0019087biological_processsymbiont-mediated transformation of host cell
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
ACYS97
ACYS99
ACYS145
AHOH197

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BE8 A 401
ChainResidue
ASER139
APHE154
AARG155
AALA156
AALA157
AVAL158
ACYS159
AHOH238
AHIS57
AARG123
AILE132
AGLY137
ASER138

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 901
ChainResidue
CCYS97
CCYS99
CCYS145
CHOH190

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"description":"Charge relay system; for serine protease NS3 activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01166","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues22
DetailsRegion: {"description":"NS3-binding","evidences":[{"source":"UniProtKB","id":"P27958","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rgq
ChainResidueDetails
AASP81
ASER139
AGLY137
AHIS57

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rgq
ChainResidueDetails
CASP81
CSER139
CGLY137
CHIS57

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PDB entries from 2025-12-17

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