› 3vp6

X-ray diffraction
2.1Å resolution

Structural characterization of Glutamic Acid Decarboxylase; insights into the mechanism of autoinactivation

Released:
DOI: 10.2210/pdb3vp6/pdb
PDB entry 3vp6 coloured by chain, front view.
PDB entry 3vp6 coloured by chain, side view.
PDB entry 3vp6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization on the mechanism of auto-inactivation for Human Glutamic Acid Decarboxylase.
Langendorf CG, Tuck KL, Key TL, Fenalti G, Pike RN, Rosado CJ, Wong AS, Buckle AM, Law RH, Whisstock JC
Biosci. Rep. (2012)
PMID: 23126365

Function and Biology Details

Reaction catalysed: 
L-glutamate = 4-aminobutanoate + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189179 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate decarboxylase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 511 amino acids
Theoretical weight: 58.43 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q99259 (Residues: 90-594; Coverage: 85%)
Gene names: GAD, GAD1, GAD67
Sequence domains: Pyridoxal-dependent decarboxylase conserved domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand HLD 2 x HLD
Ligand GOL 2 x GOL
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P21
Unit cell:
a: 86.006Å b: 64.084Å c: 102.646Å
α: 90° β: 108.14° γ: 90°
R-values:
R R work R free
0.199 0.197 0.234
Expression system: Saccharomyces cerevisiae

Quick links

Citations

4 review citations

Structural Basis for Allostery in PLP-dependent Enzymes.
Tran et al. (2022)
3 more

2 mentions without citation

Structural characterization of the mechanism through which human glutamic acid decarboxylase auto-activates.
Langendorf et al. (2013)
1 more