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

Benny Danilo Belviso.

SASDW74 – Aromatic-L-amino-acid decarboxylase L353P bound to pyridoxal 5'-phosphate (PLP)

Aromatic-L-amino-acid decarboxylase (L353P)
MWexperimental 109 kDa
MWexpected 107 kDa
VPorod 152 nm3
log I(s) 1.67×10-1 1.67×10-2 1.67×10-3 1.67×10-4
Aromatic-L-amino-acid decarboxylase (L353P) small angle scattering data  s, nm-1
ln I(s)
Aromatic-L-amino-acid decarboxylase (L353P) Guinier plot ln 1.68×10-1 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Aromatic-L-amino-acid decarboxylase (L353P) Kratky plot 1.104 0 3 sRg
p(r)
Aromatic-L-amino-acid decarboxylase (L353P) pair distance distribution function Rg: 2.9 nm 0 Dmax: 8.8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Aromatic-L-amino-acid decarboxylase (L353P) DAMMIN model

Synchrotron SAXS data from solutions of aromatic-L-amino-acid decarboxylase (L353P) bound to pyridoxal 5'-phosphate in 50 mM HEPES, pH 7.4 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 4 mg/ml was injected at a 0.16 ml/min flow rate onto a Shodex KW403-4F column at 20°C. 620 successive 3 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: Data used to calculate p(r) have been significantly truncated at both low- and high-s.

Aromatic-L-amino-acid decarboxylase (L353P) (AADC)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   53.6 kDa
 
UniProt   P20711 (1-478)
Sequence   FASTA