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
| 3.6.4.13 |
RNA helicase.
based on mapping to UniProt P27958
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).
|
| 3.4.21.98 |
Hepacivirin.
based on mapping to UniProt P27958
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.
|
| 2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt P27958
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.
|
| 3.6.1.15 |
Nucleoside-triphosphate phosphatase.
based on mapping to UniProt P27958
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 P27958
|
UniProtKB Entries (2)
| P27958 |
POLG_HCVH
Hepatitis C virus (isolate H)
Genome polyprotein
|
| O39914 |
O39914_9HEPC
Hepacivirus C
Non-structural protein 4a/b
|
PDB Structure
| PDB | 1N1L |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Pyrrolidine-5,5-trans-lactams. 2. The use of X-ray Crystal Structure Data in the Optimisation of P3 and P4 Substituents
Org.Lett.
|