Chlorine in PDB 1l7x: Human Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700

All present enzymatic activity of Human Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700:
2.4.1.1;

The structure of Human Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700, PDB code: 1l7x was solved by J.L.Ekstrom, T.A.Pauly, M.D.Carty, W.C.Soeller, J.Culp, D.E.Danley, D.J.Hoover, J.L.Treadway, E.M.Gibbs, R.J.Fletterick, Y.S.N.Day, D.G.Myszka, V.L.Rath, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.39 / 2.30
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	124.072, 124.072, 122.849, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 25.1

The binding sites of Chlorine atom in the Human Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700 (pdb code 1l7x). 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 Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700, PDB code: 1l7x:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl862 b:21.3 occ:1.00 CL1 A:700862 0.0 21.3 1.0 C4 A:700862 1.7 21.5 1.0 C3 A:700862 2.7 22.9 1.0 C5 A:700862 2.8 20.9 1.0 O A:ARG60 3.3 23.7 1.0 CG2 A:VAL64 3.5 20.7 1.0 CG A:ARG60 3.6 23.9 1.0 CB A:LEU63 3.8 26.6 1.0 N A:VAL64 3.9 24.6 1.0 CE3 A:TRP67 3.9 25.1 1.0 C6 A:700862 4.0 20.4 1.0 C2 A:700862 4.1 23.4 1.0 CZ3 A:TRP67 4.2 25.0 1.0 C A:ARG60 4.2 23.9 1.0 CA A:VAL64 4.2 23.3 1.0 CD1 A:LEU63 4.3 27.8 1.0 C A:LEU63 4.4 27.1 1.0 CD A:ARG60 4.4 24.4 1.0 CB A:VAL64 4.5 24.3 1.0 C1 A:700862 4.5 21.7 1.0 O A:HOH2015 4.6 22.7 1.0 CG A:PRO229 4.6 20.2 1.0 CA A:LEU63 4.6 25.8 1.0 CG A:LEU63 4.7 28.1 1.0 CB A:ARG60 4.7 24.5 1.0 CA A:ARG60 4.7 23.7 1.0 NE A:ARG60 4.9 23.2 1.0 CB A:PRO229 5.0 20.8 1.0 N A:LEU63 5.0 27.3 1.0

Chlorine binding site 2 out of 2 in the Human Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Liver Glycogen Phosphorylase B Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403,700 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1862 b:26.0 occ:1.00 CL1 B:7001862 0.0 26.0 1.0 C4 B:7001862 1.7 23.4 1.0 C3 B:7001862 2.7 21.4 1.0 C5 B:7001862 2.8 22.6 1.0 O B:ARG60 3.3 26.4 1.0 CG2 B:VAL64 3.5 23.0 1.0 CB B:LEU63 3.6 27.8 1.0 CG B:ARG60 3.6 27.3 1.0 N B:VAL64 3.8 23.9 1.0 CE3 B:TRP67 3.8 22.9 1.0 C6 B:7001862 4.0 19.3 1.0 C2 B:7001862 4.1 19.7 1.0 CZ3 B:TRP67 4.1 24.5 1.0 CD1 B:LEU63 4.2 25.4 1.0 CA B:VAL64 4.2 22.9 1.0 C B:LEU63 4.2 25.4 1.0 C B:ARG60 4.3 26.6 1.0 CA B:LEU63 4.5 25.2 1.0 CD B:ARG60 4.5 25.7 1.0 CG B:LEU63 4.5 27.3 1.0 CB B:VAL64 4.5 25.5 1.0 O B:HOH2390 4.5 40.1 1.0 C1 B:7001862 4.5 20.4 1.0 CB B:ARG60 4.8 29.3 1.0 CG B:PRO229 4.8 25.0 1.0 CA B:ARG60 4.8 27.3 1.0 N B:LEU63 4.9 26.4 1.0 CG2 A:VAL40 4.9 29.0 1.0 O B:LEU63 4.9 23.5 1.0 CD2 B:TRP67 5.0 24.4 1.0 CG1 A:VAL40 5.0 29.2 1.0

J.L.Ekstrom, T.A.Pauly, M.D.Carty, W.C.Soeller, J.Culp, D.E.Danley, D.J.Hoover, J.L.Treadway, E.M.Gibbs, R.J.Fletterick, Y.S.Day, D.G.Myszka, V.L.Rath. Structure-Activity Analysis of the Purine Binding Site of Human Liver Glycogen Phosphorylase. Chem.Biol. V. 9 915 2002.
ISSN: ISSN 1074-5521
PubMed: 12204691
DOI: 10.1016/S1074-5521(02)00186-2