Structure of PDB 2a4q Chain A

Receptor sequence

>2a4qA (length=181)

APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCING
VCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHA
VGLFRAAVCTRGVAKAVDFIPVENLETTMRS

3D structure

• PDB: 2a4q Synthesis and Biological Activity of Macrocyclic Inhibitors of Hepatitis C Virus (HCV) NS3 Protease
• Chain: A
• Resolution: 2.45 Å

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: 3.6.4.13: 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 I35 V36 S37 R62 T63 I64 A65 V107 R109	T4 A5 Y6 A7 Q8 Q9 T10 R11 C16 T19 S20 E30 E32 V33 I35 V36 S37 R62 T63 I64 A65 V107 R109
BS02	peptide	A	T4 A5 Y6 A7	T4 A5 Y6 A7
BS03	ZN	A	C97 C99 C145	C97 C99 C145
BS04	FNH	A	Q41 T42 H57 K136 G137 S139 R155 A156 A157 C159 D168	Q41 T42 H57 K136 G137 S139 R155 A156 A157 C159 D168	PDBbind-CN: -logKd/Ki=7.18,Ki=0.066uM

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
• GO:0097264 self proteolysis

Cellular Component

• GO:0016020 membrane
• GO:0033644 host cell membrane
• GO:0044423 virion component

External links

• PDB: RCSB:2a4q, PDBe:2a4q, PDBj:2a4q
• PDBsum: 2a4q
• PubMed: 16112859
• UniProt: Q91RS4