› 2jqv

Solution NMR

Solution structure At3g28950.1 from Arabidopsis thaliana

Released:
DOI: 10.2210/pdb2jqv/pdb
PDB entry 2jqv coloured by chain, ensemble of 20 models, front view.
PDB entry 2jqv coloured by chain, ensemble of 20 models, side view.
PDB entry 2jqv coloured by chain, ensemble of 20 models, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Solution structure of At3g28950 from Arabidopsis thaliana.
de la Cruz NB, Peterson FC, Volkman BF
Proteins 71 546-51 (2008)
PMID: 18214976

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192389 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein AIG2 C Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.6 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9MBH1 (Residues: 2-165; Coverage: 99%)
Gene names: AIG2C, At3g28950, K5K13.6
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
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: Escherichia coli

Quick links

Citations

1 citations in other articles

A gamma-glutamyl transpeptidase-independent pathway of glutathione catabolism to glutamate via 5-oxoproline in Arabidopsis.
Ohkama-Ohtsu et al. (2008)

2 mentions without citation

Structure and function of allophanate hydrolase.
Fan et al. (2013)
1 more