CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.1740 | first zn-finger domain of poly(adp-ribose) polymerase-1 |
|
3.30.1740.10 | Zinc finger, PARP-type |
Domain Context
CATH Clusters
| Superfamily | Zinc finger, PARP-type |
| Functional Family | Poly [ADP-ribose] polymerase |
Enzyme Information
| 2.4.2.- |
Pentosyltransferases.
based on mapping to UniProt P09874
|
| 2.4.2.30 |
NAD(+) ADP-ribosyltransferase.
based on mapping to UniProt P09874
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D- ribosyl)(n+1)-acceptor.
-!- The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP- ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
|
UniProtKB Entries (1)
| P09874 |
PARP1_HUMAN
Homo sapiens
Poly [ADP-ribose] polymerase 1
|
PDB Structure
| PDB | 4DQY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for DNA damage-dependent poly(ADP-ribosyl)ation by human PARP-1.
Science
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