Structure of PDB 3lox Chain A

Receptor sequence

>3loxA (length=181) [Search protein sequence]

APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCING
VCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHA
VGLFRAAVCTRGVAKAVDFIPVENLETTMRS

3D structure

PDB

3lox The introduction of P4 substituted 1-methylcyclohexyl groups into Boceprevir: a change in direction in the search for a second generation HCV NS3 protease inhibitor.

Chain

Resolution

2.65 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H57 D81 G137 S139
Catalytic site (residue number reindexed from 1)	H57 D81 G137 S139
Enzyme Commision number	3.4.21.98: hepacivirin. 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	A	T4 A5 Y6 A7 Q8 Q9 T10 R11 C16 T19 S20 E30 E32 V33 Q34 I35 V36 S37 R62 T63 I64 A65 R109	T4 A5 Y6 A7 Q8 Q9 T10 R11 C16 T19 S20 E30 E32 V33 Q34 I35 V36 S37 R62 T63 I64 A65 R109
BS02	peptide	A	T4 A5 Y6 A7 Q8	T4 A5 Y6 A7 Q8
BS03	ZN	A	C97 C145	C97 C145
BS04	MCX	A	H57 R123 I132 L135 G137 S139 F154 R155 A156 A157 D168	H57 R123 I132 L135 G137 S139 F154 R155 A156 A157 D168	PDBbind-CN: -logKd/Ki=8.10,Ki=8nM

Gene Ontology

	Molecular Function
GO:0008236	serine-type peptidase activity

	Biological Process
GO:0006508	proteolysis
GO:0019087	transformation of host cell by virus

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:3lox, PDBe:3lox, PDBj:3lox
PDBsum	3lox
PubMed	20303756
UniProt	Q9ELS8

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