PDBe 5egg

X-ray diffraction
1.76Å resolution

Crystal structure of human ubiquitin-conjugating enzyme UBCH5C

Released:
Source organism: Homo sapiens
Primary publication:
Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c.
OpenAccess logo Acta Pharm Sin B 7 390-394 (2017)
PMID: 28540177

Function and Biology Details

Reactions 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
(1a) S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [(E3-independent) E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-[(E3-independent) ubiquitin-conjugating enzyme]-L-cysteine
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 D3 Chain: A
Molecule details ›
Chain: A
Length: 156 amino acids
Theoretical weight: 17.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61077 (Residues: 1-147; Coverage: 100%)
Gene names: UBC5C, UBCH5C, UBE2D3
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: SSRF BEAMLINE BL17U
Unit cell:
a: 28.17Å b: 66.28Å c: 76.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.253
Expression system: Escherichia coli