› 3juc

X-ray diffraction
1.2Å resolution

Human gamma-glutamylamine cyclotransferase complex with 5-oxoproline

Released:
DOI: 10.2210/pdb3juc/pdb
PDB entry 3juc coloured by chain, front view.
PDB entry 3juc coloured by chain, side view.
PDB entry 3juc 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

2 bound ligands:
Ligand PCA 1 x PCA
Ligand NO3 2 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P212121
Unit cell:
a: 36.247Å b: 42.478Å c: 84.814Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 0.117 0.148
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

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

7 mentions without citation

Tetrazoles via Multicomponent Reactions.
Neochoritis et al. (2019)
6 more