› 3rzu

X-ray diffraction
2.5Å resolution

The Crystal Structure of the Catalytic Domain of AMSH

Released:
DOI: 10.2210/pdb3rzu/pdb
PDB entry 3rzu coloured by chain, front view.
PDB entry 3rzu coloured by chain, side view.
PDB entry 3rzu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and thermodynamic comparison of the catalytic domain of AMSH and AMSH-LP: nearly identical fold but different stability.
Davies CW, Paul LN, Kim MI, Das C
J Mol Biol 413 416-29 (2011)
PMID: 21888914

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-131958 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
STAM-binding protein Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 187 amino acids
Theoretical weight: 20.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O95630 (Residues: 243-424; Coverage: 43%)
Gene names: AMSH, STAMBP
Sequence domains: JAB1/Mov34/MPN/PAD-1 ubiquitin protease
Structure domains: Cytidine Deaminase, domain 2

Ligands and Environments

1 bound ligand:
Ligand ZN 14 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 203.491Å b: 67.362Å c: 113.165Å
α: 90° β: 112.44° γ: 90°
R-values:
R R work R free
0.195 0.193 0.229
Expression system: Escherichia coli BL21

Quick links

Citations

10 review citations

Deubiquitylases from genes to organism.
Clague et al. (2013)
9 more

8 mentions without citation

Mechanisms orchestrating the enzymatic activity and cellular functions of deubiquitinases.
Estavoyer et al. (2022)
7 more