› 2zgg

X-ray diffraction
2Å resolution

Asn-hydroxylation stabilises the ankyrin repeat domain fold

Released:
DOI: 10.2210/pdb2zgg/pdb
PDB entry 2zgg coloured by chain, front view.
PDB entry 2zgg coloured by chain, side view.
PDB entry 2zgg coloured by chain, top view.
Source organism: Synthetic construct
Primary publication:
Asparagine beta-hydroxylation stabilizes the ankyrin repeat domain fold.
Kelly L, McDonough MA, Coleman ML, Ratcliffe PJ, Schofield CJ
Mol Biosyst 5 52-8 (2009)
PMID: 19081931

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-163381 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3 repeat synthetic ankyrin Chain: A
Molecule details ›
Chain: A
Length: 92 amino acids
Theoretical weight: 9.73 KDa
Source organism: Synthetic construct
Expression system: Not provided
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

2 bound ligands:
Ligand CD 1 x CD
Ligand CO 2 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P3121
Unit cell:
a: 48.959Å b: 48.959Å c: 79.042Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.212 0.212 0.238
Expression system: Not provided

Quick links

Citations

12 review citations

Inhibition of 2-oxoglutarate dependent oxygenases.
Rose et al. (2011)
11 more

1 mention without citation

Notch receptor-ligand binding and activation: insights from molecular studies.
Chillakuri et al. (2012)