› 3e46

X-ray diffraction
1.86Å resolution

Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington interacting protein 2) M172A mutant

Released:
DOI: 10.2210/pdb3e46/pdb
PDB entry 3e46 coloured by chain, front view.
PDB entry 3e46 coloured by chain, side view.
PDB entry 3e46 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).
Wilson RC, Hughes RC, Flatt JW, Meehan EJ, Ng JD, Twigg PD
Acta Crystallogr Sect F Struct Biol Cryst Commun 65 440-4 (2009)
PMID: 19407372

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 K Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 28.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61086 (Residues: 1-200; Coverage: 100%)
Gene names: HIP2, LIG, UBE2K
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I4
Unit cell:
a: 134.49Å b: 134.49Å c: 38.404Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

E2s: structurally economical and functionally replete.
Wenzel et al. (2011)
6 other articles

7 mentions without citation

Huntingtin Ubiquitination Mechanisms and Novel Possible Therapies to Decrease the Toxic Effects of Mutated Huntingtin.
Fiorillo et al. (2021)
6 more