Structure of PDB 5epy Chain A

Receptor sequence
>5epyA (length=198) [Search protein sequence]
HMASMKKKGSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEG
EVQIVSTATQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKD
LVGWQAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRP
ISYLKGSAGGPLLCPAGHAVGIFRTAVSTRGVAKAVDFIPVESLETTM
3D structure
PDB5epy Structural and Thermodynamic Effects of Macrocyclization in HCV NS3/4A Inhibitor MK-5172.
ChainA
Resolution2.3 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 3.6.4.13: 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 ZN A C1097 C1099 C1145 H1149 C116 C118 C164 H168
BS02 5R2 A Q1041 F1043 Y1056 H1057 V1078 D1081 I1132 K1136 G1137 A1139 F1154 R1155 T1156 A1157 Q60 F62 Y75 H76 V97 D100 I151 K155 G156 A158 F173 R174 T175 A176 PDBbind-CN: -logKd/Ki=7.40,Kd=39.9nM
Gene Ontology
Molecular Function
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0019062 virion attachment to host cell
GO:0019087 transformation of host cell by virus
GO:0046718 symbiont entry into host cell
Cellular Component
GO:0016020 membrane
GO:0033644 host cell membrane
GO:0044423 virion component

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5epy, PDBe:5epy, PDBj:5epy
PDBsum5epy
PubMed26682473
UniProtC1KIK8

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