CATH Domain 2k2dA00

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.20	Single Sheet
	2.20.28	Rubrerythrin, domain 2
	2.20.28.10

Domain Context

CATH Clusters

Superfamily	2.20.28.10
Functional Family	CHY zinc finger domain-containing protein

Enzyme Information

2.3.2.27

RING-type E3 ubiquitin transferase.

based on mapping to UniProt Q96PM5

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.

-!- The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.

UniProtKB Entries (1)

Q96PM5

ZN363_HUMAN

Homo sapiens

RING finger and CHY zinc finger domain-containing protein 1

PDB Structure

PDB	2K2D
External Links	PDBSum Proteopedia
Method	SOLUTION NMR
Organism	Escherichia
Primary Citation	Molecular basis of Pirh2-mediated p53 ubiquitylation. Sheng, Y., Laister, R.C., Lemak, A., Wu, B., Tai, E., Duan, S., Lukin, J., Sunnerhagen, M., Srisailam, S., Karra, M., Benchimol, S., Arrowsmith, C.H. Nat.Struct.Mol.Biol.