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1NS3

STRUCTURE OF HCV PROTEASE (BK STRAIN)

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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 190
ChainResidue
ACYS97
ATHR98
ACYS99
ACYS145
AHIS149

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 690
ChainResidue
BCYS97
BCYS99
BCYS145
BSER147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916
ChainResidueDetails
AHIS57
AASP81
BHIS57
BASP81

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891
ChainResidueDetails
ASER139
BSER139

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891
ChainResidueDetails
ACYS97
ACYS99
BCYS97
BCYS99

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916
ChainResidueDetails
ACYS145
AHIS149
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

224004

PDB entries from 2024-08-21

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