CATH Domain 3eydA01

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.40	Beta Barrel
	2.40.10	Thrombin, subunit H
	2.40.10.120

Domain Context

CATH Clusters

Superfamily	2.40.10.120
Functional Family

Enzyme Information

3.6.1.15	Nucleoside-triphosphate phosphatase. based on mapping to UniProt P26664 NTP + H(2)O = NDP + phosphate. -!- The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria. -!- Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD. -!- The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
3.4.22.-	Cysteine endopeptidases. based on mapping to UniProt P26664
3.6.4.13	RNA helicase. based on mapping to UniProt P26664 ATP + H(2)O = ADP + phosphate. -!- RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. -!- Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity. -!- Some helicases unwind DNA as well as RNA. -!- May be identical with EC 3.6.4.12 (DNA helicase).
2.7.7.48	RNA-directed RNA polymerase. based on mapping to UniProt P26664 Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). -!- Catalyzes RNA-template-directed extension of the 3'-end of an RNA strand by one nucleotide at a time. -!- Can initiate a chain de novo. -!- See also EC 2.7.7.6.
3.4.21.98	Hepacivirin. based on mapping to UniProt P26664 Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'. -!- Encoded by the genome of the viruses of the hepatitis C group, and contributes to the maturation of the precursor polyproteins. -!- The enzyme is greatly activated by binding of the 54-residue NS4A 'cofactor' protein also derived from the viral polyprotein. -!- Belongs to peptidase family S29.

UniProtKB Entries (1)

POLG_HCV1

Hepatitis C virus (isolate 1)

Genome polyprotein

PDB Structure

PDB	3EYD
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Potent inhibitors of HCV-NS3 protease derived from boronic acids. Venkatraman, S., Wu, W., Prongay, A., Girijavallabhan, V., George Njoroge, F. Bioorg.Med.Chem.Lett.