Chlorine in PDB 3ddw: Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055

All present enzymatic activity of Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055:
2.4.1.1;

The structure of Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055, PDB code: 3ddw was solved by R.T.Nolte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.63 / 1.90
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	124.368, 124.368, 123.621, 90.00, 90.00, 120.00
R / Rfree (%)	15.3 / 18.6

The binding sites of Chlorine atom in the Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055 (pdb code 3ddw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055, PDB code: 3ddw:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl905 b:29.9 occ:1.00 CL1 A:055905 0.0 29.9 1.0 C30 A:055905 1.8 23.4 1.0 C29 A:055905 2.7 23.7 1.0 C25 A:055905 2.8 23.3 1.0 N24 A:055905 3.1 21.9 1.0 N22 A:055905 3.3 23.5 1.0 C23 A:055905 3.4 22.0 1.0 O14 A:055905 3.5 23.0 1.0 CE B:LYS41 3.6 22.3 1.0 CE2 A:PHE196 3.8 23.4 1.0 C28 A:055905 4.0 23.4 1.0 CD B:LYS41 4.0 23.0 1.0 C11 A:055905 4.0 23.6 1.0 C26 A:055905 4.1 24.0 1.0 CZ A:PHE196 4.2 22.4 1.0 CG2 B:VAL45 4.3 21.5 1.0 CZ A:ARG193 4.4 23.5 1.0 O A:HOH1131 4.4 32.7 1.0 C5 A:055905 4.5 23.1 1.0 NE A:ARG193 4.5 22.3 1.0 O33 A:055905 4.5 19.7 1.0 NH1 A:ARG193 4.5 22.2 1.0 C27 A:055905 4.5 23.5 1.0 N12 A:055905 4.5 25.0 1.0 C13 A:055905 4.6 26.6 1.0 O B:HOH2239 4.6 37.4 1.0 NZ B:LYS41 4.7 24.2 1.0 CD A:ARG193 4.7 23.0 1.0 C4 A:055905 4.8 23.6 1.0 NH2 A:ARG193 4.8 25.5 1.0 OE2 A:GLU195 4.8 32.9 1.0 CB B:VAL45 5.0 22.7 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Glycogen Phosphorylase Complexed with An Anthranilimide Based Inhibitor GSK055 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl906 b:30.4 occ:1.00 CL1 B:055906 0.0 30.4 1.0 C30 B:055906 1.8 24.8 1.0 C29 B:055906 2.7 25.7 1.0 C25 B:055906 2.8 25.2 1.0 N24 B:055906 3.1 22.9 1.0 N22 B:055906 3.3 25.1 1.0 C23 B:055906 3.3 23.1 1.0 O14 B:055906 3.5 24.6 1.0 CE A:LYS41 3.7 26.6 1.0 CD A:LYS41 3.7 25.8 1.0 CE2 B:PHE196 3.8 30.6 1.0 C11 B:055906 4.0 25.7 1.0 CZ B:PHE196 4.0 29.6 1.0 C28 B:055906 4.0 25.4 1.0 C26 B:055906 4.1 25.7 1.0 CG2 A:VAL45 4.3 23.7 1.0 O33 B:055906 4.3 20.1 1.0 C5 B:055906 4.3 25.2 1.0 CZ B:ARG193 4.4 24.9 1.0 N12 B:055906 4.4 27.2 1.0 NE B:ARG193 4.5 25.2 1.0 C27 B:055906 4.6 25.1 1.0 C4 B:055906 4.6 25.0 1.0 NH2 B:ARG193 4.6 26.1 1.0 C13 B:055906 4.6 30.4 1.0 NH1 B:ARG193 4.7 25.8 1.0 O B:HOH2103 4.7 43.6 1.0 O A:HOH1545 4.7 41.0 1.0 NZ A:LYS41 4.8 27.6 1.0 CB A:VAL45 4.9 24.8 1.0 O A:VAL40 4.9 18.3 1.0 CD B:ARG193 5.0 24.9 1.0 CD2 B:PHE196 5.0 29.1 1.0

S.A.Thomson, P.Banker, D.M.Bickett, J.A.Boucheron, H.L.Carter, D.C.Clancy, J.P.Cooper, S.H.Dickerson, D.M.Garrido, R.T.Nolte, A.J.Peat, L.R.Sheckler, S.M.Sparks, F.X.Tavares, L.Wang, T.Y.Wang, J.E.Weiel. Anthranilimide Based Glycogen Phosphorylase Inhibitors For the Treatment of Type 2 Diabetes. Part 3: X-Ray Crystallographic Characterization, Core and Urea Optimization and in Vivo Efficacy. Bioorg.Med.Chem.Lett. V. 19 1177 2009.
ISSN: ISSN 0960-894X
PubMed: 19138846
DOI: 10.1016/J.BMCL.2008.12.085