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4A1V

Co-Complex structure of NS3-4A protease with the optimized inhibitory peptide CP5-46A-4D5E

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 CL A 1180
ChainResidue
AARG11
AGLY12
AGLY15
APRO70

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K A 1181
ChainResidue
ASER61
AHOH2024

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 1181
ChainResidue
BLEU13
BGLY-14
BGLN9
BGLY12

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 1182
ChainResidue
BARG11
BGLY12
BGLY15
BPRO70
BHOH2012

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:0000305|PubMed:8389908, ECO:0000305|PubMed:8392606, ECO:0000305|PubMed:9060645
ChainResidueDetails
AHIS57
BHIS57

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8389908, ECO:0000305|PubMed:8392606
ChainResidueDetails
AASP81
BASP81

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166
ChainResidueDetails
ASER139
BSER139

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:9060645
ChainResidueDetails
ACYS97
ACYS99
ACYS145
AHIS149
BCYS97
BCYS99
BCYS145
BHIS149

222926

PDB entries from 2024-07-24

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