Chlorine in PDB 2q5l: X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp

All present enzymatic activity of X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp:
4.1.1.43;

The structure of X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp, PDB code: 2q5l was solved by W.Versees, S.Spaepen, M.D.Wood, F.J.Leeper, J.Vanderleyden, J.Steyaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.50 / 1.85
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.978, 179.050, 120.858, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 20.4

The structure of X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp (pdb code 2q5l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp, PDB code: 2q5l:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl3004 b:18.0 occ:1.00 OH A:TYR400 3.0 14.2 1.0 OG1 A:THR236 3.1 16.7 1.0 N A:VAL211 3.4 17.0 1.0 N A:ILE279 3.5 19.6 1.0 O A:HOH4036 3.5 23.7 1.0 CB A:CYS210 3.6 18.9 1.0 CE2 A:TYR400 3.7 16.6 1.0 CB A:VAL211 3.7 15.3 1.0 CG1 A:VAL211 3.7 15.9 1.0 CB A:THR236 3.7 17.6 1.0 CA A:ALA278 3.8 17.8 1.0 CZ A:TYR400 3.8 16.2 1.0 CG2 A:THR236 4.0 17.5 1.0 CB A:MET238 4.0 21.9 1.0 C A:ALA278 4.2 19.2 1.0 CB A:ALA278 4.2 16.2 1.0 CA A:VAL211 4.2 16.1 1.0 CA A:CYS210 4.3 18.3 1.0 CB A:ILE279 4.3 19.5 1.0 C A:CYS210 4.3 18.0 1.0 O A:GLY277 4.4 20.0 1.0 CA A:ILE279 4.5 20.1 1.0 O A:ILE279 4.5 21.6 1.0 CG A:MET238 4.5 26.6 1.0 CG1 A:ILE279 4.7 18.7 1.0 SG A:CYS210 4.7 19.2 1.0 N A:MET238 4.8 19.7 1.0 N A:ALA278 4.8 16.8 1.0 CA A:MET238 4.9 20.6 1.0 CD1 A:ILE279 4.9 19.2 1.0 C A:ILE279 5.0 21.4 1.0 C A:GLY277 5.0 18.6 1.0 CD2 A:TYR400 5.0 17.1 1.0

Chlorine binding site 2 out of 2 in the X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of X-Ray Structure of Phenylpyruvate Decarboxylase in Complex with 2-(1- Hydroxyethyl)-3-Deaza-Thdp within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl3003 b:17.6 occ:1.00 OG1 B:THR236 3.1 15.9 1.0 OH B:TYR400 3.1 21.0 1.0 N B:ILE279 3.4 17.4 1.0 N B:VAL211 3.4 16.7 1.0 CB B:CYS210 3.6 16.8 1.0 CE2 B:TYR400 3.7 19.3 1.0 CB B:VAL211 3.7 18.0 1.0 O B:HOH4051 3.8 20.0 1.0 CG1 B:VAL211 3.8 18.6 1.0 CB B:THR236 3.8 15.1 1.0 CA B:ALA278 3.8 15.6 1.0 CZ B:TYR400 3.9 20.9 1.0 CB B:MET238 4.0 24.5 1.0 CG2 B:THR236 4.1 16.2 1.0 C B:ALA278 4.1 17.5 1.0 CB B:ALA278 4.2 17.5 1.0 CA B:VAL211 4.2 16.1 1.0 CB B:ILE279 4.3 17.6 1.0 CA B:CYS210 4.3 15.8 1.0 O B:GLY277 4.3 17.3 1.0 C B:CYS210 4.4 15.4 1.0 CA B:ILE279 4.4 19.2 1.0 O B:ILE279 4.5 23.9 1.0 CG B:MET238 4.5 29.9 1.0 CG1 B:ILE279 4.6 16.8 1.0 N B:MET238 4.7 22.6 1.0 CA B:MET238 4.7 23.2 1.0 CD1 B:ILE279 4.7 18.6 1.0 SG B:CYS210 4.8 19.0 1.0 N B:ALA278 4.9 14.9 1.0 C B:ILE279 4.9 22.7 1.0 C B:GLY277 5.0 15.7 1.0 C B:MET238 5.0 22.7 1.0

W.Versees, S.Spaepen, M.D.Wood, F.J.Leeper, J.Vanderleyden, J.Steyaert. Molecular Mechanism of Allosteric Substrate Activation in A Thiamine Diphosphate-Dependent Decarboxylase. J.Biol.Chem. V. 282 35269 2007.
ISSN: ISSN 0021-9258
PubMed: 17905741
DOI: 10.1074/JBC.M706048200