Chlorine in PDB 3cej: Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865

All present enzymatic activity of Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865:
2.4.1.1;

The structure of Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865, PDB code: 3cej was solved by K.U.Wendt, M.K.Dreyer, O.Anderka, T.Klabunde, P.Loenze, E.Defossa, D.Schmoll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.47 / 3.30
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	123.270, 123.270, 121.880, 90.00, 90.00, 120.00
R / Rfree (%)	17.6 / 27.1

The structure of Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865 also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Chlorine atom in the Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865 (pdb code 3cej). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865, PDB code: 3cej:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl833 b:52.5 occ:1.00 CL8 A:AVF833 0.0 52.5 1.0 C5 A:AVF833 1.7 53.0 1.0 C6 A:AVF833 2.7 53.0 1.0 C4 A:AVF833 2.7 53.9 1.0 C7 A:AVF833 3.1 53.9 1.0 O A:TRP67 3.2 48.1 1.0 O20 A:AVF833 3.3 54.2 1.0 C A:TRP67 3.4 48.5 1.0 CG A:GLN71 3.4 51.3 1.0 N A:ILE68 3.6 48.6 1.0 CB A:GLN71 3.6 51.0 1.0 CG A:TRP67 3.7 48.5 1.0 CA A:ILE68 3.7 48.4 1.0 CD1 A:TRP67 3.7 48.3 1.0 N10 A:AVF833 3.9 54.7 1.0 C1 A:AVF833 4.0 53.0 1.0 C3 A:AVF833 4.0 53.4 1.0 CD2 A:TRP67 4.0 48.4 1.0 CB A:TRP67 4.1 48.6 1.0 NE1 A:TRP67 4.1 48.4 1.0 CE2 A:TRP67 4.3 48.4 1.0 CA A:TRP67 4.3 48.6 1.0 C2 A:AVF833 4.5 53.0 1.0 CG1 A:ILE68 4.5 48.1 1.0 C A:ILE68 4.7 48.6 1.0 CG1 B:VAL40 4.7 46.9 1.0 O A:ILE68 4.7 48.4 1.0 CE3 A:TRP67 4.7 47.9 1.0 CB A:ILE68 4.7 48.0 1.0 OG1 A:THR240 4.8 42.2 1.0 C11 A:AVF833 4.8 55.0 1.0 O B:VAL40 4.8 46.9 1.0 CD A:GLN71 4.9 51.5 1.0 CA A:GLN71 4.9 51.1 1.0 N12 A:AVF833 5.0 55.4 1.0

Chlorine binding site 2 out of 2 in the Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Glycogen Phosphorylase (Tense State) in Complex with the Allosteric Inhibitor AVE2865 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl833 b:56.4 occ:1.00 CL8 B:AVF833 0.0 56.4 1.0 C5 B:AVF833 1.7 56.4 1.0 C6 B:AVF833 2.7 56.6 1.0 C4 B:AVF833 2.7 55.4 1.0 CG B:GLN71 3.0 47.3 1.0 C7 B:AVF833 3.1 55.1 1.0 O B:TRP67 3.2 48.5 1.0 O20 B:AVF833 3.3 53.6 1.0 CB B:GLN71 3.4 47.7 1.0 CD1 B:TRP67 3.7 49.2 1.0 CG B:TRP67 3.8 48.6 1.0 C B:TRP67 3.8 48.4 1.0 NE1 B:TRP67 3.8 49.6 1.0 C3 B:AVF833 4.0 56.0 1.0 C1 B:AVF833 4.0 56.0 1.0 CD2 B:TRP67 4.0 48.0 1.0 CE2 B:TRP67 4.0 48.8 1.0 N10 B:AVF833 4.1 53.7 1.0 CA B:ILE68 4.3 47.8 1.0 N B:ILE68 4.3 48.1 1.0 CD B:GLN71 4.4 46.0 1.0 CB B:TRP67 4.4 48.9 1.0 C2 B:AVF833 4.5 55.8 1.0 OG1 B:THR240 4.6 39.2 1.0 CG1 A:VAL40 4.6 54.5 1.0 CA B:TRP67 4.7 48.7 1.0 CE3 B:TRP67 4.8 47.9 1.0 CG1 B:ILE68 4.8 47.0 1.0 CZ2 B:TRP67 4.8 48.8 1.0 CA B:GLN71 4.9 47.9 1.0 NE2 B:GLN71 4.9 45.5 1.0 C11 B:AVF833 5.0 53.9 1.0

O.Anderka, P.Loenze, T.Klabunde, M.K.Dreyer, E.Defossa, K.U.Wendt, D.Schmoll. Thermodynamic Characterization of Allosteric Glycogen Phosphorylase Inhibitors. Biochemistry V. 47 4683 2008.
ISSN: ISSN 0006-2960
PubMed: 18373353
DOI: 10.1021/BI702397D