2znv

X-ray diffraction
1.6Å resolution

Crystal structure of human AMSH-LP DUB domain in complex with Lys63-linked ubiquitin dimer

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
AMSH-like protease Chains: A, D
Molecule details ›
Chains: A, D
Length: 178 amino acids
Theoretical weight: 19.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96FJ0 (Residues: 264-436; Coverage: 40%)
Gene names: AMSHLP, KIAA1373, STAMBPL1
Sequence domains: JAB1/Mov34/MPN/PAD-1 ubiquitin protease
Structure domains: Cytidine Deaminase, domain 2
Ubiquitin Chains: B, E
Molecule details ›
Chains: B, E
Length: 76 amino acids
Theoretical weight: 8.6 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG50 (Residues: 609-684; Coverage: 10%)
Gene name: Ubc
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Ubiquitin Chains: C, F
Molecule details ›
Chains: C, F
Length: 77 amino acids
Theoretical weight: 8.69 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG50 (Residues: 609-684; Coverage: 10%)
Gene name: Ubc
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 38.089Å b: 97.363Å c: 87.894Å
α: 90° β: 97.49° γ: 90°
R-values:
R R work R free
0.185 0.184 0.215
Expression system: Escherichia coli