5jkn

X-ray diffraction
3Å resolution

Crystal structure of deubiquitinase MINDY-1

Released:

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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-185404 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin carboxyl-terminal hydrolase MINDY-1 Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 32.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8N5J2 (Residues: 110-384; Coverage: 59%)
Gene names: FAM63A, KIAA1390, MINDY1
Sequence domains: MINDY deubiquitinase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P4122
Unit cell:
a: 99.671Å b: 99.671Å c: 165.123Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.242
Expression system: Escherichia coli BL21(DE3)