Structure of PDB 2xcn Chain A

Receptor sequence

>2xcnA (length=180)

APITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCING
VCWTVYHGAGTRTIASPKGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCG
SSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHA
VGLFRAAVCTRGVAKAVDFIPVENLETTMR

3D structure

• PDB: 2xcn Synthesis and Evaluation of Novel Alpha-Amino Cyclic Boronates as Inhibitors of Hcv Ns3 Protease.
• Chain: A
• Resolution: 3.02 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 S20 E30 E32 V33 Q34 I35 V36 S37 R62 T63 I64 A65	T4 A5 Y6 A7 Q8 Q9 T10 R11 S20 E30 E32 V33 Q34 I35 V36 S37 R62 T63 I64 A65
BS02	peptide	A	T4 A5 Y6	T4 A5 Y6
BS03	C8D	A	H57 R123 G137 S139 F154 R155 A156 A157 D168	H57 R123 G137 S139 F154 R155 A156 A157 D168	PDBbind-CN: -logKd/Ki=6.92,IC50=0.12uM
BS04	MG	A	A5 A111	A5 A111
BS05	ZN	A	C97 C99 C145	C97 C99 C145

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:2xcn, PDBe:2xcn, PDBj:2xcn
• PDBsum: 2xcn
• PubMed: 20493689
• UniProt: Q91RS4