› 2zfy

X-ray diffraction
1.69Å resolution

Crystal structure of human Otubain 1

Released:
DOI: 10.2210/pdb2zfy/pdb
PDB entry 2zfy coloured by chain, front view.
PDB entry 2zfy coloured by chain, side view.
PDB entry 2zfy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis and specificity of human otubain 1-mediated deubiquitination.
Edelmann MJ, Iphöfer A, Akutsu M, Altun M, di Gleria K, Kramer HB, Fiebiger E, Dhe-Paganon S, Kessler BM
Biochem J 418 379-90 (2009)
PMID: 18954305

Function and Biology Details

Reaction catalysed: 
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).
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188504 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin thioesterase OTUB1 Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 27.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96FW1 (Residues: 40-271; Coverage: 86%)
Gene names: HSPC263, OTB1, OTU1, OTUB1
Sequence domains: Peptidase C65 Otubain
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 81.25Å b: 50.886Å c: 54.722Å
α: 90° β: 101.96° γ: 90°
R-values:
R R work R free
0.195 0.192 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

34 review citations

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

18 mentions without citation

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