Structure of PDB 5eqq Chain A

Receptor sequence
>5eqqA (length=190) [Search protein sequence]
GSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEGEVQIVSTA
TQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKDLVGWQAPQ
GSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSA
GGPLLCPAGHAVGIFRAAVCTRGVAKAVDFIPVESLETTM
3D structure
PDB5eqq Structural and Thermodynamic Effects of Macrocyclization in HCV NS3/4A Inhibitor MK-5172.
ChainA
Resolution1.65 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) H68 D92 G148 A150
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 C108 C110 C156 H160
BS02 5RS A F1043 H1057 V1078 D1081 L1135 K1136 G1137 A1139 F1154 R1155 A1156 A1157 F54 H68 V89 D92 L146 K147 G148 A150 F165 R166 A167 A168 MOAD: Kd=6.7nM
PDBbind-CN: -logKd/Ki=8.17,Kd=6.7nM
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:5eqq, PDBe:5eqq, PDBj:5eqq
PDBsum5eqq
PubMed26682473
UniProtC1KIK8

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