› 1yla

X-ray diffraction
2.4Å resolution

Ubiquitin-conjugating enzyme E2-25 kDa (Huntington interacting protein 2)

Released:
DOI: 10.2210/pdb1yla/pdb
PDB entry 1yla coloured by chain, front view.
PDB entry 1yla coloured by chain, side view.
PDB entry 1yla coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of E2-25K/UBB+1 interaction leading to proteasome inhibition and neurotoxicity.
Ko S, Kang GB, Song SM, Lee JG, Shin DY, Yun JH, Sheng Y, Cheong C, Jeon YH, Jung YK, Arrowsmith CH, Avvakumov GV, Dhe-Paganon S, Yoo YJ, Eom SH, Lee W
J Biol Chem 285 36070-80 (2010)
PMID: 20826778

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158206 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 K Chains: A, B
Molecule details ›
Chains: A, B
Length: 202 amino acids
Theoretical weight: 22.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61086 (Residues: 1-200; Coverage: 100%)
Gene names: HIP2, LIG, UBE2K
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 37.831Å b: 55.022Å c: 61.762Å
α: 64.19° β: 74.61° γ: 69.89°
R-values:
R R work R free
0.225 0.225 0.269
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Oxidative stress, neurodegeneration, and the balance of protein degradation and protein synthesis.
Dasuri et al. (2013)
8 more

8 mentions without citation

Structural basis of generic versus specific E2-RING E3 interactions in protein ubiquitination.
Gundogdu et al. (2019)
7 more