6z90

X-ray diffraction
3.59Å resolution

Crystal structure of MINDY1 mutant-P138A

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: 32.01 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

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P4122
Unit cell:
a: 98.649Å b: 98.649Å c: 166.073Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.258
Expression system: Escherichia coli