› 2g0q

Solution NMR

Solution structure of At5g39720.1 from Arabidopsis thaliana

Released:
DOI: 10.2210/pdb2g0q/pdb
PDB entry 2g0q coloured by chain, ensemble of 20 models, front view.
PDB entry 2g0q coloured by chain, ensemble of 20 models, side view.
PDB entry 2g0q coloured by chain, ensemble of 20 models, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family.
Lytle BL, Peterson FC, Tyler EM, Newman CL, Vinarov DA, Markley JL, Volkman BF
Acta Crystallogr Sect F Struct Biol Cryst Commun 62 490-3 (2006)
PMID: 16754964

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190337 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AIG2-like protein A Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 20.13 KDa
Source organism: Arabidopsis thaliana
Expression system: Not provided
UniProt:
  • Canonical: Q9FIX2 (Residues: 2-165; Coverage: 99%)
Gene names: AIG2LA, At5g39720, MIJ24.180, MKM21.1, MKM21.3, MKM21_10
Sequence domains: Gamma-glutamyl cyclotransferase, AIG2-like
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVENT
Expression system: Not provided

Quick links

Citations

6 citation in other articles

Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Ziarek et al. (2011)
5 more

4 mentions without citation

Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism.
Oakley et al. (2010)
3 more