5jqs

X-ray diffraction
2.65Å resolution

Crystal structure of deubiquitinase MINDY-1 in complex with Ubiquitin

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:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-158847 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
UniProt:
  • Canonical: Q8N5J2 (Residues: 110-384; Coverage: 59%)
Gene names: FAM63A, KIAA1390, MINDY1
Sequence domains: MINDY deubiquitinase
Ubiquitin Chain: D
Molecule details ›
Chain: D
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
Expression system: Bos taurus
UniProt:
  • Canonical: P62992 (Residues: 1-76; Coverage: 49%)
Gene names: RPS27A, UBA80, UBCEP1
Sequence domains: Ubiquitin family

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6522
Unit cell:
a: 82.336Å b: 82.336Å c: 332.464Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.205 0.231
Expression systems:
  • Escherichia coli
  • Bos taurus