CATH Classification

Domain Context

CATH Clusters

Superfamily Poly(ADP-ribose) polymerase, regulatory domain
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 5A00
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Discovery of 2-[1-(4,4-Difluorocyclohexyl)Piperidin-4-Yl]-6-Fluoro-3-Oxo-2,3-Dihydro-1H-Isoindole-4-Carboxamide (Nms-P118): A Potent, Orally Available and Highly Selective Parp- 1 Inhibitor for Cancer Therapy.
Papeo, G.M.E., Posteri, H., Borghi, D., Busel, A.A., Caprera, F., Casale, E., Ciomei, M., Cirla, A., Corti, E., D'Anello, M., Fasolini, M., Forte, B., Galvani, A., Isacchi, A., Khvat, A., Krasavin, M.Y., Lupi, R., Orsini, P., Perego, R., Pesenti, E., Pezzetta, D., Rainoldi, S., Riccardi-Sirtori, F., Scolaro, A., Sola, F., Zuccotto, F., Felder, E.R., Donati, D., Montagnoli, A.
J.Med.Chem.