Chlorine in PDB 3rbl: Crystal Structure of Human Aromatic L-Amino Acid Decarboxylase (Aadc) in the Apo Form

All present enzymatic activity of Crystal Structure of Human Aromatic L-Amino Acid Decarboxylase (Aadc) in the Apo Form:
4.1.1.28;

The structure of Crystal Structure of Human Aromatic L-Amino Acid Decarboxylase (Aadc) in the Apo Form, PDB code: 3rbl was solved by G.Giardina, R.Montioli, S.Gianni, B.Cellini, A.Paiardini, C.Borrivoltattorni, F.Cutruzzola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 3.24
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	179.640, 179.640, 74.950, 90.00, 90.00, 90.00
R / Rfree (%)	23.6 / 29.4

The binding sites of Chlorine atom in the Crystal Structure of Human Aromatic L-Amino Acid Decarboxylase (Aadc) in the Apo Form (pdb code 3rbl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Aromatic L-Amino Acid Decarboxylase (Aadc) in the Apo Form, PDB code: 3rbl:

Chlorine binding site 1 out of 1 in the Crystal Structure of Human Aromatic L-Amino Acid Decarboxylase (Aadc) in the Apo Form


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Aromatic L-Amino Acid Decarboxylase (Aadc) in the Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl481 b:56.5 occ:1.00 NZ B:LYS303 3.2 47.3 1.0 NE1 B:TRP304 3.6 48.8 1.0 CB B:TYR274 3.7 42.8 1.0 N B:ALA275 3.8 41.5 1.0 CD B:LYS303 3.9 47.3 1.0 CE B:LYS303 4.0 48.4 1.0 CA B:ALA275 4.1 40.8 1.0 C B:TYR274 4.2 42.1 1.0 SG B:CYS249 4.2 41.3 1.0 CB B:ALA275 4.3 40.8 1.0 CD1 B:LEU406 4.3 38.2 1.0 CA B:TYR274 4.5 42.5 1.0 CE2 B:TRP304 4.6 48.3 1.0 CD1 B:TRP304 4.6 48.6 1.0 CZ2 B:TRP304 4.7 48.9 1.0 CG B:TYR274 4.8 44.1 1.0 O B:TYR274 4.9 42.4 1.0 CD2 B:TYR274 4.9 46.1 1.0

G.Giardina, R.Montioli, S.Gianni, B.Cellini, A.Paiardini, C.B.Voltattorni, F.Cutruzzola. Open Conformation of Human Dopa Decarboxylase Reveals the Mechanism of Plp Addition to Group II Decarboxylases. Proc.Natl.Acad.Sci.Usa V. 108 20514 2011.
ISSN: ISSN 0027-8424
PubMed: 22143761
DOI: 10.1073/PNAS.1111456108