5mn9

X-ray diffraction
2.05Å resolution

Crystal structure of MINDY-1 tMIU in complex with K48-diUb

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-158848 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin Chains: A, B
Molecule details ›
Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P62992 (Residues: 1-76; Coverage: 49%)
Gene names: RPS27A, UBA80, UBCEP1
Sequence domains: Ubiquitin family
Ubiquitin carboxyl-terminal hydrolase MINDY-1 Chain: C
Molecule details ›
Chain: C
Length: 44 amino acids
Theoretical weight: 4.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8N5J2 (Residues: 388-426; Coverage: 8%)
Gene names: FAM63A, KIAA1390, MINDY1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: I41
Unit cell:
a: 55.14Å b: 55.14Å c: 105.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.223
Expression system: Escherichia coli BL21(DE3)