› 2znr

X-ray diffraction
1.2Å resolution

Crystal structure of the DUB domain of human AMSH-LP

Released:
DOI: 10.2210/pdb2znr/pdb
PDB entry 2znr coloured by chain, front view.
PDB entry 2znr coloured by chain, side view.
PDB entry 2znr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains.
Sato Y, Yoshikawa A, Yamagata A, Mimura H, Yamashita M, Ookata K, Nureki O, Iwai K, Komada M, Fukai S
Nature 455 358-62 (2008)
PMID: 18758443

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AMSH-like protease Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 19.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96FJ0 (Residues: 264-436; Coverage: 40%)
Gene names: AMSHLP, KIAA1373, STAMBPL1
Sequence domains: JAB1/Mov34/MPN/PAD-1 ubiquitin protease
Structure domains: Cytidine Deaminase, domain 2

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand PR 1 x PR
Ligand EDO 7 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P65
Unit cell:
a: 81.865Å b: 81.865Å c: 64.693Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 0.149 0.165
Expression system: Escherichia coli

Quick links

Citations

65 review citations

The ubiquitin code.
Komander et al. (2012)
64 more

17 mentions without citation

Regulation of proteolysis by human deubiquitinating enzymes.
Eletr et al. (2014)
16 more