CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.1840 | main proteinase (3clpro) structure, domain 3 |
|
1.10.1840.10 | main proteinase (3clpro) structure, domain 3 |
Domain Context
CATH Clusters
| Superfamily | main proteinase (3clpro) structure, domain 3 |
| Functional Family |
Enzyme Information
| 2.7.7.48 |
RNA-directed RNA polymerase.
based on mapping to UniProt P0C6Y3
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.
|
| 3.1.13.- |
Exoribonucleases producing 5'-phosphomonoesters.
based on mapping to UniProt P0C6Y3
|
| 2.1.1.- |
Methyltransferases.
based on mapping to UniProt P0C6Y3
|
| 3.1.-.- |
Acting on ester bonds.
based on mapping to UniProt P0C6Y3
|
| 3.6.4.12 |
DNA helicase.
based on mapping to UniProt P0C6Y3
ATP + H(2)O = ADP + phosphate.
-!- DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA. -!- Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15). -!- Some helicases unwind DNA as well as RNA (4,9). -!- May be identical with EC 3.6.4.13 (RNA helicase).
|
| 3.6.4.13 |
RNA helicase.
based on mapping to UniProt P0C6Y3
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).
|
| 3.4.22.- |
Cysteine endopeptidases.
based on mapping to UniProt P0C6Y3
|
UniProtKB Entries (1)
| P0C6Y3 |
R1AB_IBVM
Avian infectious bronchitis virus (strain M41)
Replicase polyprotein 1ab
|
PDB Structure
| PDB | 2Q6D |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structures of two coronavirus main proteases: implications for substrate binding and antiviral drug design.
J.Virol.
|
