Structure of PDB 5epn Chain A

Receptor sequence
>5epnA (length=197) [Search protein sequence]
MASMKKKGSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEGE
VQIVSTATQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKDL
VGWQAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPI
SYLKGSSGGPLLCPAGHAVGIFRAAVSTRGVAKAVDFIPVESLETTM
3D structure
PDB5epn 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
[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) H75 D99 G155 S157
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 C115 C117 C163 H167
BS02 5R2 A Q1041 F1043 H1057 V1078 D1081 K1136 G1137 S1139 F1154 R1155 A1156 A1157 Q59 F61 H75 V96 D99 K154 G155 S157 F172 R173 A174 A175 MOAD: Kd=2.2nM
PDBbind-CN: -logKd/Ki=8.66,Kd=2.2nM
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:5epn, PDBe:5epn, PDBj:5epn
PDBsum5epn
PubMed26682473
UniProtC1KIK8

[Back to BioLiP]