Aromatic-L-amino-acid decarboxylase (AADC) L353P - pyridoxal 5'-phosphate bound form

Benny Danilo Belviso.

SASDW84 – Aromatic-L-amino-acid decarboxylase R347Q bound to pyridoxal 5'-phosphate (PLP)

Aromatic-L-amino-acid decarboxylase (R347Q)
MWexperimental 114 kDa
MWexpected 108 kDa
VPorod 220 nm3
log I(s) 5.64×102 5.64×101 5.64×100 5.64×10-1
Aromatic-L-amino-acid decarboxylase (R347Q) small angle scattering data  s, nm-1
ln I(s)
Aromatic-L-amino-acid decarboxylase (R347Q) Guinier plot ln 5.65×102 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Aromatic-L-amino-acid decarboxylase (R347Q) Kratky plot 1.104 0 √3 sRg
p(r)
Aromatic-L-amino-acid decarboxylase (R347Q) pair distance distribution function Rg: 3.6 nm 0 Dmax: 14.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Aromatic-L-amino-acid decarboxylase (R347Q) DAMMIN model
Synchrotron SAXS data from solutions of aromatic-L-amino-acid decarboxylase (R347Q) bound to pyridoxal 5'-phosphate in 50 mM HEPES, 100 µM pyridoxal 5'-phosphate, pH 7.4 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 5.4 and 5.4 mg/ml were measured at 4°C. Four successive 5 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Pyridoxal 5'-phosphate: https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405. CAUTION: Potentially aggregated.

Aromatic-L-amino-acid decarboxylase (R347Q) (AADC)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   53.9 kDa
 
UniProt   P20711 (1-478)
Sequence   FASTA