6sak

X-ray diffraction
2Å resolution

Structure of the OTULINcat C129A - SNX27 PDZ domain complex.

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).
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-188380 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin thioesterase otulin Chains: A, B
Molecule details ›
Chains: A, B
Length: 275 amino acids
Theoretical weight: 31.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96BN8 (Residues: 80-352; Coverage: 78%)
Gene names: FAM105B, OTULIN
Sequence domains: Peptidase family C101
Sorting nexin-27 Chains: C, D
Molecule details ›
Chains: C, D
Length: 96 amino acids
Theoretical weight: 10.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96L92 (Residues: 40-135; Coverage: 18%)
Gene names: KIAA0488, My014, SNX27
Sequence domains: PDZ domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P1
Unit cell:
a: 54.645Å b: 62.912Å c: 72.017Å
α: 65.132° β: 85.976° γ: 85.38°
R-values:
R R work R free
0.217 0.215 0.253
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli