CATH Classification

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 2L31
External Links
Method SOLUTION NMR
Organism
Primary Citation
The DNA-binding domain of human PARP-1 interacts with DNA single-strand breaks as a monomer through its second zinc finger.
Eustermann, S., Videler, H., Yang, J.C., Cole, P.T., Gruszka, D., Veprintsev, D., Neuhaus, D.
J.Mol.Biol.
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