› 5jg6

X-ray diffraction
2Å resolution

APC11-Ubv shows role of noncovalent RING-Ubiquitin interactions in processive multiubiquitination and Ubiquitin chain elongation by APC/C

Released:
DOI: 10.2210/pdb5jg6/pdb
PDB entry 5jg6 coloured by chain, front view.
PDB entry 5jg6 coloured by chain, side view.
PDB entry 5jg6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C.
Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA
Cell 165 1440-1453 (2016)
PMID: 27259151

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143290 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Anaphase-promoting complex subunit 11 Chains: A, D
Molecule details ›
Chains: A, D
Length: 70 amino acids
Theoretical weight: 8.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NYG5 (Residues: 17-84; Coverage: 81%)
Gene names: ANAPC11, HSPC214
Sequence domains: Anaphase-promoting complex subunit 11 RING-H2 finger
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)
Ubiquitin Chains: B, C
Molecule details ›
Chains: B, C
Length: 84 amino acids
Theoretical weight: 9.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CG47 (Residues: 76-154; Coverage: 35%)
Gene name: UBB
Sequence domains: Ubiquitin family

Ligands and Environments

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 131.066Å b: 35.193Å c: 72.768Å
α: 90° β: 120.42° γ: 90°
R-values:
R R work R free
0.187 0.185 0.22
Expression system: Escherichia coli

Quick links

Citations

30 review citations

Ubiquitin Ligases: Structure, Function, and Regulation.
Zheng et al. (2017)
29 more

4 mentions without citation

Structural Diversity of Ubiquitin E3 Ligase.
Toma-Fukai et al. (2021)
3 more