› 1ymp

X-ray diffraction
2.2Å resolution

The Crystal Structure of a Partial Mouse Notch-1 Ankyrin Domain: Repeats 4 Through 7 Preserve an Ankyrin Fold

Released:
DOI: 10.2210/pdb1ymp/pdb
PDB entry 1ymp coloured by chain, front view.
PDB entry 1ymp coloured by chain, side view.
PDB entry 1ymp coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold.
Lubman OY, Kopan R, Waksman G, Korolev S
Protein Sci 14 1274-81 (2005)
PMID: 15802643

Function and Biology Details

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-169617 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Notch 1 intracellular domain Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 15.08 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01705 (Residues: 1971-2105; Coverage: 5%)
Gene names: Motch, Notch1
Sequence domains:
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P31
Unit cell:
a: 75.789Å b: 75.789Å c: 45.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.309
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Functional diversity of ankyrin repeats in microbial proteins.
Al-Khodor et al. (2010)
5 more

5 mentions without citation

The molecular logic of Notch signaling--a structural and biochemical perspective.
Gordon et al. (2008)
4 more