CATH Domain 5uqvA02

CATH Classification

Level	CATH Code	Description
	2	Mainly Beta
	2.20	Single Sheet
	2.20.210	ubp-family deubiquitinating enzyme fold
	2.20.210.10	ubp-family deubiquitinating enzyme superfamily

Domain Context

CATH Clusters

Superfamily	ubp-family deubiquitinating enzyme superfamily
Functional Family

Enzyme Information

3.4.19.12

Ubiquitinyl hydrolase 1.

based on mapping to UniProt Q93009

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

-!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12.

UniProtKB Entries (1)

Q93009

UBP7_HUMAN

Homo sapiens

Ubiquitin carboxyl-terminal hydrolase 7

PDB Structure

PDB	5UQV
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	USP7 small-molecule inhibitors interfere with ubiquitin binding. Kategaya, L., Di Lello, P., Rouge, L., Pastor, R., Clark, K.R., Drummond, J., Kleinheinz, T., Lin, E., Upton, J.P., Prakash, S., Heideker, J., McCleland, M., Ritorto, M.S., Alessi, D.R., Trost, M., Bainbridge, T.W., Kwok, M.C.M., Ma, T.P., Stiffler, Z., Brasher, B., Tang, Y., Jaishankar, P., Hearn, B.R., Renslo, A.R., Arkin, M.R., Cohen, F., Yu, K., Peale, F., Gnad, F., Chang, M.T., Klijn, C., Blackwood, E., Martin, S.E., Forrest, W.F., Ernst, J.A., Ndubaku, C., Wang, X., Beresini, M.H., Tsui, V., Schwerdtfeger, C., Blake, R.A., Murray, J., Maurer, T., Wertz, I.E. Nature