› 1q56

Solution NMR

NMR structure of the B0 isoform of the agrin G3 domain in its Ca2+ bound state

Released:
DOI: 10.2210/pdb1q56/pdb
PDB entry 1q56 coloured by chain, ensemble of 15 models, front view.
PDB entry 1q56 coloured by chain, ensemble of 15 models, side view.
PDB entry 1q56 coloured by chain, ensemble of 15 models, top view.
Source organism: Gallus gallus
Primary publication:
Modulation of agrin function by alternative splicing and Ca2+ binding.
Stetefeld J, Alexandrescu AT, Maciejewski MW, Jenny M, Rathgeb-Szabo K, Schulthess T, Landwehr R, Frank S, Ruegg MA, Kammerer RA
Structure 12 503-15 (2004)
PMID: 15016366

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152071 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Agrin C-terminal 22 kDa fragment Chain: A
Molecule details ›
Chain: A
Length: 195 amino acids
Theoretical weight: 21.33 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P31696 (Residues: 1870-2081; Coverage: 9%)
Gene names: AGRIN, AGRN
Sequence domains: Laminin G domain
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Torsion angle dynamics (Dyana 1.5) followed by simulated annealing (X-Plor 3.851)
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.
Iozzo et al. (2015)
13 more

3 mentions without citation

Mechanical strength of 17,134 model proteins and cysteine slipknots.
Sikora et al. (2009)
2 more