› 3rch

X-ray diffraction
2.8Å resolution

Crystal structure of Human aromatic L-amino acid decarboxylase (AADC) in the open conformation with LLP and PLP bound to Chain-A and Chain-B respectively

Released:
DOI: 10.2210/pdb3rch/pdb
PDB entry 3rch coloured by chain, front view.
PDB entry 3rch coloured by chain, side view.
PDB entry 3rch 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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149042 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aromatic-L-amino-acid decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 480 amino acids
Theoretical weight: 54.19 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:
Aromatic-L-amino-acid decarboxylase Chain: B
Molecule details ›
Chain: 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


Cofactor: Ligand PLP 1 x PLP
No bound ligands
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41212
Unit cell:
a: 177Å b: 177Å c: 74.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.266 0.2 0.259
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

6 mentions without citation

Discovery and characterization of gut microbiota decarboxylases that can produce the neurotransmitter tryptamine.
Williams et al. (2014)
5 more