PDBsum entry 4dm9

Hydrolase, ligase/inhibitor

PDB id: 4dm9

Contents

Protein chain

223 a.a.

Ligands

PHQ-VAL-ALA-GME-CF0 ×2

Waters ×42

PDB id:

4dm9

Name:

Hydrolase, ligase/inhibitor

Title:

The crystal structure of ubiquitin carboxy-terminal hydrolase l1 (uchl1) bound to a tripeptide fluoromethyl ketone z-vae(ome)-fmk

Structure:

Ubiquitin carboxyl-terminal hydrolase isozyme l1. Chain: a, b. Synonym: uch-l1, neuron cytoplasmic protein 9.5, pgp 9.5, pgp9.5, ubiquitin thioesterase l1. Engineered: yes. Tripeptide fluoromethyl ketone inhibitor z-vae(ome)-fmk. Chain: x, y. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: uchl1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes

Resolution:

2.35Å R-factor: 0.200 R-free: 0.250

Authors:

C.W.Davies,J.Chaney,G.Korbel,D.Ringe,G.A.Petsko,H.Ploegh,C.Das

Key ref:

C.W.Davies et al. (2012). The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK). Bioorg Med Chem Lett, 22, 3900-3904. PubMed id: 22617491

Date:

07-Feb-12 Release date: 23-May-12

Protein chains

P09936  (UCHL1_HUMAN) -  Ubiquitin carboxyl-terminal hydrolase isozyme L1 from Homo sapiens

Seq: 223 a.a.

Struc: 223 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.19.12 - ubiquitinyl hydrolase 1.
• Reaction: Thiol-dependent hydrolysis of ester, thiolester, 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).

Bioorg Med Chem Lett 22:3900-3904 (2012)

PubMed id: 22617491

The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK).

C.W.Davies, J.Chaney, G.Korbel, D.Ringe, G.A.Petsko, H.Ploegh, C.Das.

ABSTRACT

No abstract given.