Structure of PDB 5etx Chain D

Receptor sequence
>5etxD (length=187) [Search protein sequence]
KGSVVIVGRINLYAQQTRGEEGCQETSQTGRDKNQVEGEVQIVSTATQTF
LATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKDLVGWQAPQGSRS
LTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPL
LCPAGHAVGIFRTAVSTRGVAKAVDFIPVESLETTMR
3D structure
PDB5etx Structural and Thermodynamic Effects of Macrocyclization in HCV NS3/4A Inhibitor MK-5172.
ChainD
Resolution2.35 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 S1139
Catalytic site (residue number reindexed from 1) H64 D88 G144 S146
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 D C1097 C1099 C1145 C104 C106 C152
BS02 5RS D Q1041 F1043 H1057 L1135 K1136 G1137 S1139 F1154 R1155 T1156 A1157 Q48 F50 H64 L142 K143 G144 S146 F161 R162 T163 A164
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5etx, PDBe:5etx, PDBj:5etx
PDBsum5etx
PubMed26682473
UniProtC1KIK8

[Back to BioLiP]