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1BT7

THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0019087biological_processtransformation of host cell by virus
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AVAL151
ACYS97
ACYS99
ACYS145

site_idCTS
Number of Residues3
DetailsCATALYTIC SITE
ChainResidue
AHIS57
AASP81
ASER139

site_idZNB
Number of Residues3
DetailsZINC BINDING SITE
ChainResidue
ACYS97
ACYS99
ACYS145

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916
ChainResidueDetails
AHIS57
AASP81

site_idSWS_FT_FI2
Number of Residues1
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

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891
ChainResidueDetails
ACYS97
ACYS99

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916
ChainResidueDetails
ACYS145
AHIS149

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by protease NS2 => ECO:0000255|PROSITE-ProRule:PRU01030
ChainResidueDetails
APRO2

217705

PDB entries from 2024-03-27

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