› 3jud

X-ray diffraction
0.98Å resolution

Human gamma-glutamylamine cyclotransferase, E82Q mutant

Released:
DOI: 10.2210/pdb3jud/pdb
PDB entry 3jud coloured by chain, front view.
PDB entry 3jud coloured by chain, side view.
PDB entry 3jud coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification and characterization of gamma-glutamylamine cyclotransferase, an enzyme responsible for gamma-glutamyl-epsilon-lysine catabolism.
Oakley AJ, Coggan M, Board PG
J Biol Chem 285 9642-9648 (2010)
PMID: 20110353

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-189764 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gamma-glutamylaminecyclotransferase Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 17.35 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BVM4 (Residues: 1-153; Coverage: 100%)
Gene names: A2LD1, GGACT
Sequence domains: Gamma-glutamyl cyclotransferase, AIG2-like
Structure domains: Gamma-glutamyl cyclotransferase-like

Ligands and Environments

1 bound ligand:
Ligand NO3 3 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 36.307Å b: 42.443Å c: 84.764Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.18
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Emerging regulatory paradigms in glutathione metabolism.
Liu et al. (2014)
4 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