Structure of PDB 3su2 Chain A

Receptor sequence
>3su2A (length=198) [Search protein sequence]
HMASMKKKGSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEG
EVQIVSTATQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKD
LVGWQAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRP
ISYLKGSAGGPLLCPAGHAVGIFRTAVSTRGVAKAVDFIPVESLETTM
3D structure
PDB3su2 The Molecular Basis of Drug Resistance against Hepatitis C Virus NS3/4A Protease Inhibitors.
ChainA
Resolution1.496 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H1057 D1081 G1137 A1139
Catalytic site (residue number reindexed from 1) H76 D100 G156 A158
Enzyme Commision number 3.4.21.98: hepacivirin.
3.6.1.15: nucleoside-triphosphate phosphatase.
3.6.4.13: RNA helicase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 TSV A Q1041 F1043 H1057 V1078 D1081 L1135 K1136 G1137 A1139 F1154 R1155 T1156 A1157 Q60 F62 H76 V97 D100 L154 K155 G156 A158 F173 R174 T175 A176 MOAD: Ki=44.8nM
PDBbind-CN: -logKd/Ki=7.35,Ki=44.8nM
BS02 ZN A C1097 C1099 C1145 H1149 C116 C118 C164 H168
Gene Ontology
Molecular Function
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019087 transformation of host cell by virus

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Molecular Function
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Biological Process
External links
PDB RCSB:3su2, PDBe:3su2, PDBj:3su2
PDBsum3su2
PubMed22910833
UniProtA8DG50

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