Structure of PDB 5eqr Chain A

Receptor sequence
>5eqrA (length=198) [Search protein sequence]
HMASMKKKGSVVIVGRINLSGDTAYAQQTRGEEGCQETSQTGRDKNQVEG
EVQIVSTATQTFLATSINGVLWTVYHGAGTRTIASPKGPVTQMYTNVDKD
LVGWQAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSTGSLLSPRP
LSYLKGSSGGPLLCPAGHAVGIFRAAVSTRGVAKAVQFIPVESLETTM
3D structure
PDB5eqr Molecular and Dynamic Mechanism Underlying Drug Resistance in Genotype 3 Hepatitis C NS3/4A Protease.
ChainA
Resolution1.96 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 S1139
Catalytic site (residue number reindexed from 1) H76 D100 G156 S158
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 TSV A F1043 H1057 D1081 L1135 K1136 G1137 S1139 F1154 R1155 A1156 A1157 Q1168 F62 H76 D100 L154 K155 G156 S158 F173 R174 A175 A176 Q187
BS02 ZN A C1097 C1099 C1145 H1149 C116 C118 C164 H168
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:5eqr, PDBe:5eqr, PDBj:5eqr
PDBsum5eqr
PubMed27512818
UniProtA0A0B4WYC6

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