1 keywords

CATH Domain 5ngfB02

CATH Classification

Level CATH Code Description
Class 2 Mainly Beta
Architecture 2.20 Single Sheet
Topology 2.20.210 ubp-family deubiquitinating enzyme fold
Homologous Superfamily 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 5NGF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Molecular basis of USP7 inhibition by selective small-molecule inhibitors.
Turnbull, A.P., Ioannidis, S., Krajewski, W.W., Pinto-Fernandez, A., Heride, C., Martin, A.C.L., Tonkin, L.M., Townsend, E.C., Buker, S.M., Lancia, D.R., Caravella, J.A., Toms, A.V., Charlton, T.M., Lahdenranta, J., Wilker, E., Follows, B.C., Evans, N.J., Stead, L., Alli, C., Zarayskiy, V.V., Talbot, A.C., Buckmelter, A.J., Wang, M., McKinnon, C.L., Saab, F., McGouran, J.F., Century, H., Gersch, M., Pittman, M.S., Marshall, C.G., Raynham, T.M., Simcox, M., Stewart, L.M.D., McLoughlin, S.B., Escobedo, J.A., Bair, K.W., Dinsmore, C.J., Hammonds, T.R., Kim, S., Urbe, S., Clague, M.J., Kessler, B.M., Komander, D.
Nature