Structure of PDB 2fm2 Chain A

Receptor sequence

>2fm2A (length=181) [Search protein sequence]

APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCING
VCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHA
VGLFRAAVCTRGVAKAVDFIPVENLETTMRS

3D structure

PDB

2fm2 Mutations conferring resistance to SCH6, a novel hepatitis C virus NS3/4A protease inhibitor. Reduced RNA replication fitness and partial rescue by second-site mutations

Chain

Resolution

2.7 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 S20 Q28 E30 E32 V33 I35 V36 S37 T61 R62 T63 I64 A65 R92 R109	T4 A5 Y6 A7 Q8 Q9 T10 R11 C16 S20 Q28 E30 E32 V33 I35 V36 S37 T61 R62 T63 I64 A65 R92 R109
BS02	peptide	A	T4 A5 Y6	T4 A5 Y6
BS03	ZN	A	C97 C99 C145	C97 C99 C145
BS04	3BC	A	Q41 T42 H57 I132 K136 G137 S139 F154 R155 A156 A157 D168	Q41 T42 H57 I132 K136 G137 S139 F154 R155 A156 A157 D168	PDBbind-CN: -logKd/Ki=8.15,Ki=7nM

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:2fm2, PDBe:2fm2, PDBj:2fm2
PDBsum	2fm2
PubMed	16352601
UniProt	Q9ELS8

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