Chlorine in PDB 2zb2: Human Liver Glycogen Phosphorylase A Complexed with Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide

All present enzymatic activity of Human Liver Glycogen Phosphorylase A Complexed with Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide:
2.4.1.1;

The structure of Human Liver Glycogen Phosphorylase A Complexed with Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide, PDB code: 2zb2 was solved by N.Katayama, K.Onda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.18 / 2.45
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	123.819, 123.819, 123.538, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Human Liver Glycogen Phosphorylase A Complexed with Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide (pdb code 2zb2). 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 Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide, PDB code: 2zb2:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Liver Glycogen Phosphorylase A Complexed with Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide


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 Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl850 b:26.6 occ:1.00 CL1 A:A46850 0.0 26.6 1.0 C16 A:A46850 1.7 21.5 1.0 C15 A:A46850 2.7 21.3 1.0 C14 A:A46850 2.8 18.9 1.0 CE3 A:TRP67 3.5 24.0 1.0 O A:ARG60 3.6 23.0 1.0 CB A:LEU63 3.6 21.9 1.0 CG1 A:VAL64 3.6 25.3 1.0 CG A:ARG60 3.7 24.8 1.0 CZ3 A:TRP67 3.8 25.1 1.0 N A:VAL64 3.9 26.6 1.0 C13 A:A46850 4.0 20.6 1.0 C12 A:A46850 4.1 19.1 1.0 CG A:PRO229 4.2 19.5 1.0 C A:LEU63 4.2 26.2 1.0 CD1 A:LEU63 4.3 19.1 1.0 CA A:VAL64 4.3 28.0 1.0 CD A:ARG60 4.4 25.8 1.0 CA A:LEU63 4.5 23.5 1.0 C A:ARG60 4.6 23.5 1.0 C11 A:A46850 4.6 20.5 1.0 CG A:LEU63 4.6 19.4 1.0 CB A:VAL64 4.6 27.5 1.0 O A:HOH864 4.7 19.4 1.0 CD2 A:TRP67 4.7 24.0 1.0 CB A:PRO229 4.7 20.7 1.0 O A:LEU63 4.8 28.0 1.0 CD A:PRO229 4.9 18.9 1.0 CG2 B:VAL40 4.9 25.8 1.0 CB A:ARG60 4.9 24.7 1.0 NE A:ARG60 5.0 25.5 1.0

Chlorine binding site 2 out of 2 in the Human Liver Glycogen Phosphorylase A Complexed with Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide


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 Glcose and 5- Chloro-N-[4-(1,2-Dihydroxyethyl)Phenyl]-1H-Indole-2-Carboxamide within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl850 b:30.2 occ:1.00 CL1 B:A46850 0.0 30.2 1.0 C16 B:A46850 1.6 28.7 1.0 C14 B:A46850 2.6 28.1 1.0 C15 B:A46850 2.6 27.2 1.0 O B:ARG60 3.5 20.3 1.0 CG1 B:VAL64 3.5 28.3 1.0 CG B:ARG60 3.6 25.2 1.0 CE3 B:TRP67 3.7 22.1 1.0 CB B:LEU63 3.7 24.4 1.0 CZ3 B:TRP67 3.9 21.3 1.0 N B:VAL64 3.9 26.4 1.0 C13 B:A46850 3.9 25.5 1.0 C12 B:A46850 3.9 27.7 1.0 CA B:VAL64 4.2 28.1 1.0 O B:HOH1106 4.3 15.8 1.0 C B:LEU63 4.3 25.7 1.0 CD B:ARG60 4.3 25.1 1.0 CG B:PRO229 4.4 21.6 1.0 CD1 B:LEU63 4.4 21.9 1.0 C11 B:A46850 4.4 26.7 1.0 C B:ARG60 4.5 22.4 1.0 CB B:VAL64 4.5 28.2 1.0 CA B:LEU63 4.6 25.3 1.0 CG B:LEU63 4.7 23.5 1.0 CG2 A:VAL40 4.7 26.8 1.0 NE B:ARG60 4.8 23.7 1.0 CD2 B:TRP67 4.8 23.9 1.0 CB B:ARG60 4.9 25.1 1.0 CB B:PRO229 4.9 19.1 1.0 O B:LEU63 4.9 26.9 1.0

K.Onda, T.Suzuki, R.Shiraki, Y.Yonetoku, K.Negoro, K.Momose, N.Katayama, M.Orita, T.Yamaguchi, M.Ohta, S.Tsukamoto. Synthesis of 5-Chloro-N-Aryl-1H-Indole-2-Carboxamide Derivatives As Inhibitors of Human Liver Glycogen Phosphorylase A. Bioorg.Med.Chem. V. 16 5452 2008.
ISSN: ISSN 0968-0896
PubMed: 18434170
DOI: 10.1016/J.BMC.2008.04.010