› 2kl2

Solution NMR

NMR solution structure of A2LD1 (gi:13879369)

Released:
DOI: 10.2210/pdb2kl2/pdb
PDB entry 2kl2 coloured by chain, ensemble of 20 models, front view.
PDB entry 2kl2 coloured by chain, ensemble of 20 models, side view.
PDB entry 2kl2 coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.
Serrano P, Pedrini B, Geralt M, Jaudzems K, Mohanty B, Horst R, Herrmann T, Elsliger MA, Wilson IA, Wüthrich K
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 1393-405 (2010)
PMID: 20944236

Function and Biology Details

Reaction catalysed: 
Epsilon-(gamma-L-glutamyl)-L-lysine = L-lysine + 5-oxo-L-proline
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gamma-glutamylaminecyclotransferase Chain: A
Molecule details ›
Chain: A
Length: 149 amino acids
Theoretical weight: 17.1 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q923B0 (Residues: 1-149; Coverage: 100%)
Gene names: A2ld1, Ggact
Sequence domains: Gamma-glutamyl cyclotransferase, AIG2-like
Structure domains: Gamma-glutamyl cyclotransferase-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 79%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

γ-Glutamylamines and neurodegenerative diseases.
Jeitner et al. (2013)
6 other articles

3 mentions without citation

The J-UNIO protocol for automated protein structure determination by NMR in solution.
Serrano et al. (2012)
2 more