Structure of PDB 3su5 Chain A

Receptor sequence
>3su5A (length=201) [Search protein sequence]
SHMASMKKKGSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVE
GEVQIVSTATQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDK
DLVGWQAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPR
PISYLKGSAGGPLLCPAGHAVGIFRAAVSTRGVAKAVAFIPVESLETTMR
S
3D structure
PDB3su5 The Molecular Basis of Drug Resistance against Hepatitis C Virus NS3/4A Protease Inhibitors.
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H1057 D1081 G1137 A1139
Catalytic site (residue number reindexed from 1) H77 D101 G157 A159
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 SU3 A Q1041 F1043 H1057 D1081 L1135 K1136 G1137 A1139 F1154 R1155 A1156 A1157 Q61 F63 H77 D101 L155 K156 G157 A159 F174 R175 A176 A177 MOAD: Ki=2635nM
PDBbind-CN: -logKd/Ki=5.58,Ki=2635nM
BS02 ZN A C1097 C1099 C1145 H1149 C117 C119 C165 H169
Gene Ontology
Molecular Function
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019087 transformation of host cell by virus

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3su5, PDBe:3su5, PDBj:3su5
PDBsum3su5
PubMed22910833
UniProtA8DG50

[Back to BioLiP]