› 3rbl

X-ray diffraction
3.24Å resolution

Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the apo form

Released:
DOI: 10.2210/pdb3rbl/pdb
PDB entry 3rbl coloured by chain, front view.
PDB entry 3rbl coloured by chain, side view.
PDB entry 3rbl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases.
Giardina G, Montioli R, Gianni S, Cellini B, Paiardini A, Voltattorni CB, Cutruzzolà F
Proc Natl Acad Sci U S A 108 20514-9 (2011)
PMID: 22143761

Function and Biology Details

Reaction catalysed: 
5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149043 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aromatic-L-amino-acid decarboxylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 480 amino acids
Theoretical weight: 53.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20711 (Residues: 1-480; Coverage: 100%)
Gene names: AADC, DDC
Sequence domains: Pyridoxal-dependent decarboxylase conserved domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41212
Unit cell:
a: 179.64Å b: 179.64Å c: 74.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.236 0.294
Expression system: Escherichia coli

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Citations

13 review citations

Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.
Liang et al. (2019)
12 more

5 mentions without citation

Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases.
Giardina et al. (2011)
4 more