4wlr

X-ray diffraction
2Å resolution

Crystal Structure of mUCH37-hRPN13 CTD-hUb 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).
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-143268 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ubiquitin carboxyl-terminal hydrolase isozyme L5 Chain: A
Molecule details ›
Chain: A
Length: 328 amino acids
Theoretical weight: 37.53 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WUP7 (Residues: 1-329; Coverage: 100%)
Gene names: Uch37, Uchl5
Sequence domains:
Proteasomal ubiquitin receptor ADRM1 Chain: B
Molecule details ›
Chain: B
Length: 102 amino acids
Theoretical weight: 10.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16186 (Residues: 285-386; Coverage: 25%)
Gene names: ADRM1, GP110
Sequence domains: UCH-binding domain
Ubiquitin Chain: C
Molecule details ›
Chain: C
Length: 76 amino acids
Theoretical weight: 8.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 153-228; Coverage: 33%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 60.12Å b: 99.61Å c: 99.909Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.227
Expression system: Escherichia coli