› 1yh2

X-ray diffraction
2Å resolution

Ubiquitin-Conjugating Enzyme HSPC150

Released:
DOI: 10.2210/pdb1yh2/pdb
PDB entry 1yh2 coloured by chain, front view.
PDB entry 1yh2 coloured by chain, side view.
PDB entry 1yh2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen.
Sheng Y, Hong JH, Doherty R, Srikumar T, Shloush J, Avvakumov GV, Walker JR, Xue S, Neculai D, Wan JW, Kim SK, Arrowsmith CH, Raught B, Dhe-Paganon S
Mol Cell Proteomics 11 329-41 (2012)
PMID: 22496338

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192476 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 T Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NPD8 (Residues: 1-167; Coverage: 85%)
Gene names: HSPC150, PIG50, UBE2T
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P43212
Unit cell:
a: 54.831Å b: 54.831Å c: 183.279Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.238
Expression system: Escherichia coli

Quick links

Citations

10 review citations

E2 enzymes: more than just middle men.
Stewart et al. (2016)
9 more

11 mentions without citation

E2s: structurally economical and functionally replete.
Wenzel et al. (2011)
10 more