› 3ceg

X-ray diffraction
2.01Å resolution

Crystal structure of the UBC domain of baculoviral IAP repeat-containing protein 6

Released:
DOI: 10.2210/pdb3ceg/pdb
PDB entry 3ceg coloured by chain, front view.
PDB entry 3ceg coloured by chain, side view.
PDB entry 3ceg 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-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192523 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Baculoviral IAP repeat-containing protein 6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 37.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9NR09 (Residues: 4498-4820; Coverage: 7%)
Gene names: BIRC6, KIAA1289
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 78.199Å b: 97.815Å c: 129.888Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.211 0.252
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Mammalian HECT ubiquitin-protein ligases: biological and pathophysiological aspects.
Scheffner et al. (2014)
9 more

9 mentions without citation

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