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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_processtransformation of host cell by virus
C0006508biological_processproteolysis
C0008236molecular_functionserine-type peptidase activity
C0019087biological_processtransformation of host cell by virus
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
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166
ChainResidueDetails
AHIS57
AASP81
ASER139
CHIS57
CASP81
CSER139

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166
ChainResidueDetails
ACYS97
ACYS99
ACYS145
AHIS149
CCYS97
CCYS99
CCYS145
CHIS149

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

223532

PDB entries from 2024-08-07

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