Structure of PDB 1n1l Chain A

Receptor sequence

>1n1lA (length=180) [Search protein sequence]

APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCING
VCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHA
VGLFRAAVCTRGVTKAVDFIPVENLETTMR

3D structure

PDB

1n1l Pyrrolidine-5,5-trans-lactams. 2. The use of X-ray Crystal Structure Data in the Optimisation of P3 and P4 Substituents

Chain

Resolution

2.6 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	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)
BS01	peptide	A	T4 A5 Y6 A7 Q8 T10 R11 C16 S20 Q28 E30 E32 V33 Q34 I35 V36 S37 R62 T63 I64 W85 R109	T4 A5 Y6 A7 Q8 T10 R11 C16 S20 Q28 E30 E32 V33 Q34 I35 V36 S37 R62 T63 I64 W85 R109
BS02	peptide	A	T4 A5 Y6	T4 A5 Y6
BS03	ZN	A	C97 C99 C145	C97 C99 C145
BS04	TRL	A	F43 H57 I132 L135 G137 S139 A156 A157	F43 H57 I132 L135 G137 S139 A156 A157

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:1n1l, PDBe:1n1l, PDBj:1n1l
PDBsum	1n1l
PubMed	12465917
UniProt	P27958\|POLG_HCV77 Genome polyprotein

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