Chlorine in PDB 1l5q: Human Liver Glycogen Phosphorylase A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700

All present enzymatic activity of Human Liver Glycogen Phosphorylase A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700:
2.4.1.1;

The structure of Human Liver Glycogen Phosphorylase A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700, PDB code: 1l5q 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)	40.82 / 2.25
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	124.713, 124.713, 124.450, 90.00, 90.00, 120.00
R / Rfree (%)	20.7 / 24

The binding sites of Chlorine atom in the Human Liver Glycogen Phosphorylase A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700 (pdb code 1l5q). 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 A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700, PDB code: 1l5q:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Liver Glycogen Phosphorylase A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700


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 A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl862 b:1.3 occ:1.00 CL1 A:700862 0.0 1.3 1.0 C4 A:700862 1.7 8.2 1.0 C3 A:700862 2.7 12.6 1.0 C5 A:700862 2.7 11.2 1.0 O A:ARG60 3.4 10.0 1.0 CG A:ARG60 3.6 16.2 1.0 CB A:LEU63 3.6 16.5 1.0 CG2 A:VAL64 3.6 12.5 1.0 CE3 A:TRP67 3.8 17.9 1.0 N A:VAL64 3.8 17.5 1.0 C2 A:700862 4.0 11.9 1.0 C6 A:700862 4.0 11.6 1.0 CZ3 A:TRP67 4.1 18.7 1.0 CD1 A:LEU63 4.2 18.0 1.0 CA A:VAL64 4.2 15.9 1.0 C A:LEU63 4.3 19.2 1.0 C A:ARG60 4.4 14.2 1.0 CD A:ARG60 4.4 19.1 1.0 O B:HOH2252 4.5 26.1 1.0 CA A:LEU63 4.5 17.1 1.0 C1 A:700862 4.5 13.8 1.0 CG A:LEU63 4.5 17.3 1.0 CG A:PRO229 4.6 14.8 1.0 CB A:VAL64 4.6 15.9 1.0 CB A:ARG60 4.8 15.7 1.0 CA A:ARG60 4.8 15.4 1.0 CB A:PRO229 4.9 15.7 1.0 CD2 A:TRP67 4.9 16.9 1.0 NE A:ARG60 4.9 16.9 1.0 O A:LEU63 4.9 18.8 1.0 N A:LEU63 5.0 18.3 1.0

Chlorine binding site 2 out of 2 in the Human Liver Glycogen Phosphorylase A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700


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 A Complexed with Caffeine, N- Acetyl-Beta-D-Glucopyranosylamine, and Cp-403700 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1862 b:1.3 occ:1.00 CL1 B:7001862 0.0 1.3 1.0 C4 B:7001862 1.7 7.0 1.0 C5 B:7001862 2.7 7.9 1.0 C3 B:7001862 2.7 8.6 1.0 O B:ARG60 3.5 15.0 1.0 CG B:ARG60 3.6 17.7 1.0 CB B:LEU63 3.6 16.6 1.0 CG2 B:VAL64 3.7 15.9 1.0 CE3 B:TRP67 3.7 16.5 1.0 N B:VAL64 3.9 17.7 1.0 C6 B:7001862 4.0 8.6 1.0 CZ3 B:TRP67 4.0 18.7 1.0 C2 B:7001862 4.1 10.6 1.0 CD1 B:LEU63 4.2 17.3 1.0 CA B:VAL64 4.3 16.0 1.0 C B:LEU63 4.3 18.0 1.0 CD B:ARG60 4.4 16.0 1.0 C B:ARG60 4.4 16.1 1.0 C1 B:7001862 4.5 10.0 1.0 CA B:LEU63 4.6 17.7 1.0 CG B:LEU63 4.6 16.8 1.0 CG B:PRO229 4.6 16.8 1.0 CB B:VAL64 4.6 16.5 1.0 O A:HOH2202 4.7 22.3 1.0 CB B:ARG60 4.8 16.0 1.0 CA B:ARG60 4.8 15.4 1.0 CD2 B:TRP67 4.9 17.3 1.0 CB B:PRO229 4.9 15.8 1.0 NE B:ARG60 4.9 13.8 1.0 CG2 A:VAL40 5.0 17.6 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