Bromine in PDB 1m66: Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine

All present enzymatic activity of Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine:
1.1.1.8;

The structure of Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine, PDB code: 1m66 was solved by J.Choe, S.Suresh, G.Wisedchaisri, K.J.Kennedy, M.H.Gelb, W.G.J.Hol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.18 / 1.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	70.356, 70.356, 210.794, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 22.3

The structure of Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Bromine atom in the Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine (pdb code 1m66). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine, PDB code: 1m66:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine within 5.0Å range: probe atom residue distance (Å) B Occ A:Br401 b:63.3 occ:0.70 BR A:BCP401 0.0 63.3 0.7 BR A:BCP401 0.1 62.4 0.3 C2 A:BCP401 1.8 57.2 0.3 C2 A:BCP401 1.8 54.4 0.7 N3 A:BCP401 2.6 56.1 0.3 N1 A:BCP401 2.7 55.9 0.3 N1 A:BCP401 2.7 52.5 0.7 N3 A:BCP401 2.7 52.9 0.7 CH2 A:TRP44 3.6 32.6 1.0 CZ3 A:TRP44 3.6 33.9 1.0 CG2 A:ILE93 3.8 19.2 1.0 C4 A:BCP401 3.9 55.4 0.3 O A:HOH765 3.9 35.6 1.0 CD1 A:PHE101 3.9 23.9 1.0 CB A:PHE101 3.9 22.4 1.0 C6 A:BCP401 4.0 54.9 0.3 C4 A:BCP401 4.0 52.0 0.7 C6 A:BCP401 4.0 52.1 0.7 CB A:PHE97 4.0 26.2 1.0 CD1 A:ILE93 4.2 19.9 1.0 CG1 A:ILE93 4.3 21.2 1.0 CG A:PHE101 4.3 22.2 1.0 O A:HOH831 4.3 27.3 1.0 O A:PHE97 4.4 24.1 1.0 C5 A:BCP401 4.4 55.2 0.3 C5 A:BCP401 4.5 52.3 0.7 O A:HOH726 4.7 47.0 1.0 CB A:ILE93 4.7 20.8 1.0 CG A:PHE97 4.8 27.5 1.0 CE1 A:PHE101 4.9 24.6 1.0 CZ2 A:TRP44 4.9 33.5 1.0 CA A:PHE101 4.9 21.9 1.0 C A:PHE97 4.9 24.4 1.0 CE3 A:TRP44 4.9 31.6 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Leishmania Mexicana Gpdh Complexed with Inhibitor 2-Bromo-6-Chloro-Purine within 5.0Å range: probe atom residue distance (Å) B Occ A:Br401 b:62.4 occ:0.30 BR A:BCP401 0.0 62.4 0.3 BR A:BCP401 0.1 63.3 0.7 C2 A:BCP401 1.9 57.2 0.3 C2 A:BCP401 2.0 54.4 0.7 N1 A:BCP401 2.8 55.9 0.3 N3 A:BCP401 2.8 56.1 0.3 N3 A:BCP401 2.8 52.9 0.7 N1 A:BCP401 2.8 52.5 0.7 CZ3 A:TRP44 3.6 33.9 1.0 CH2 A:TRP44 3.6 32.6 1.0 CG2 A:ILE93 3.7 19.2 1.0 CD1 A:PHE101 3.8 23.9 1.0 CB A:PHE101 3.9 22.4 1.0 O A:HOH765 4.0 35.6 1.0 C4 A:BCP401 4.0 55.4 0.3 C6 A:BCP401 4.0 54.9 0.3 C4 A:BCP401 4.1 52.0 0.7 CD1 A:ILE93 4.1 19.9 1.0 CB A:PHE97 4.1 26.2 1.0 C6 A:BCP401 4.1 52.1 0.7 CG1 A:ILE93 4.2 21.2 1.0 CG A:PHE101 4.2 22.2 1.0 O A:HOH831 4.3 27.3 1.0 O A:PHE97 4.4 24.1 1.0 C5 A:BCP401 4.6 55.2 0.3 CB A:ILE93 4.6 20.8 1.0 C5 A:BCP401 4.6 52.3 0.7 O A:HOH726 4.7 47.0 1.0 CE1 A:PHE101 4.8 24.6 1.0 CZ2 A:TRP44 4.8 33.5 1.0 CE3 A:TRP44 4.8 31.6 1.0 CA A:PHE101 4.9 21.9 1.0 CG A:PHE97 4.9 27.5 1.0 C A:PHE97 5.0 24.4 1.0

J.Choe, S.Suresh, G.Wisedchaisri, K.J.Kennedy, M.H.Gelb, W.G.J.Hol. Anomalous Differences of Light Elements in Determining Precise Binding Modes of Ligands to Glycerol-3-Phosphate Dehydrogenase Chem.Biol. V. 9 1189 2002.
ISSN: ISSN 1074-5521
PubMed: 12445769
DOI: 10.1016/S1074-5521(02)00243-0