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:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Ubiquitin thioesterase otulin and Ubiquitin (preferred)
PDBe Complex ID:
PDB-CPX-143393 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin thioesterase otulin
Molecule details ›
Chains: A, B, E, G, I, K, M, O, Q, S, U, W
Length: 276 amino acids
Theoretical weight: 32.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Peptidase family C101
Length: 276 amino acids
Theoretical weight: 32.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q96BN8 (Residues: 79-352; Coverage: 78%)
Sequence domains: Peptidase family C101
Ubiquitin
Molecule details ›
Chains: C, D, F, H, J, L, N, P, R, T, V, X
Length: 156 amino acids
Theoretical weight: 17.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 156 amino acids
Theoretical weight: 17.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P0CG48 (Residues: 532-684; Coverage: 22%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 24-ID-C
Spacegroup:
P21212
Expression system: Escherichia coli BL21(DE3)
