Structure of PDB 2xni Chain B

Receptor sequence
>2xniB (length=153) [Search protein sequence]
QVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTN
VDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLL
SPRPISYLKGSSGGPLLCPAGHAVGLFRAAVCTRGVAKAVDFIPVENLET
TMR
3D structure
PDB2xni Novel Macrocyclic Hcv Ns3 Protease Inhibitors Derived from Alpha-Amino Cyclic Boronates.
ChainB
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D81 G137 S139
Catalytic site (residue number reindexed from 1) H30 D54 G110 S112
Enzyme Commision number 2.7.7.48: RNA-directed RNA polymerase.
3.4.21.98: hepacivirin.
3.4.22.-
3.6.1.15: nucleoside-triphosphate phosphatase.
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 peptide B V29 E32 V33 Q34 I35 V36 S37 R62 T63 A65 W85 V2 E5 V6 Q7 I8 V9 S10 R35 T36 A38 W58
BS02 ZN B C97 C99 C145 C70 C72 C118
Gene Ontology
Molecular Function
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019087 transformation of host cell by virus

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Molecular Function
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Biological Process
External links
PDB RCSB:2xni, PDBe:2xni, PDBj:2xni
PDBsum2xni
PubMed20801653
UniProtP27958|POLG_HCV77 Genome polyprotein

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