› 5din

X-ray diffraction
1.86Å resolution

Structural Basis for the Indispensable Role of a Unique Zinc Finger Motif in LNX2 Ubiquitination

Released:
DOI: 10.2210/pdb5din/pdb
PDB entry 5din coloured by chain, front view.
PDB entry 5din coloured by chain, side view.
PDB entry 5din coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the indispensable role of a unique zinc finger motif in LNX2 ubiquitination.
Nayak D, Sivaraman J
Oncotarget 6 34342-57 (2015)
PMID: 26451611

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185382 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ligand of Numb protein X 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 15.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8N448 (Residues: 20-147; Coverage: 19%)
Gene names: LNX2, PDZRN1
Sequence domains: Zinc finger, C3HC4 type (RING finger)
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

2 bound ligands:
Ligand ZN 8 x ZN
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21
Unit cell:
a: 46.969Å b: 69.399Å c: 52.249Å
α: 90° β: 115.41° γ: 90°
R-values:
R R work R free
0.193 0.19 0.232
Expression system: Escherichia coli

Quick links

Citations

2 review citations

LNX1/LNX2 proteins: functions in neuronal signalling and beyond.
Young PW. (2018)
1 more

3 mentions without citation

The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1.
Middleton et al. (2017)
2 more