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1RTL

CRYSTAL STRUCTURE OF HCV NS3 PROTEASE DOMAIN: NS4A PEPTIDE COMPLEX WITH COVALENTLY BOUND PYRROLIDINE-5,5-TRANSLACTAM INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0019087biological_processtransformation of host cell by virus
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0019087biological_processtransformation of host cell by virus
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS97
ACYS99
ACYS145
AHOH307

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BCYS97
BCYS99
BCYS145
BHOH305

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CPX A 201
ChainResidue
AHIS57
AGLY58
AILE132
ASER139
APHE154
AALA156
AALA157
AASP168
AHOH329
AGLN41

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
BHIS57
BASP81
BSER139

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166
ChainResidueDetails
ACYS97
ACYS99
ACYS145
AHIS149
BCYS97
BCYS99
BCYS145
BHIS149

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
BASP81
BSER139
BGLY137
BHIS57

223790

PDB entries from 2024-08-14

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