Fluorine in PDB 2bu6: Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands

All present enzymatic activity of Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands:
2.7.1.99;

The structure of Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands, PDB code: 2bu6 was solved by T.R.Knoechel, A.D.Tucker, C.M.Robinson, C.Phillips, W.Taylor, P.J.Bungay, S.A.Kasten, T.E.Roche, D.G.Brown, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.40
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	108.873, 108.873, 84.202, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Fluorine atom in the Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands (pdb code 2bu6). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands, PDB code: 2bu6:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands within 5.0Å range: probe atom residue distance (Å) B Occ A:F1386 b:65.0 occ:1.00 F1 A:TF21386 0.0 65.0 1.0 C18 A:TF21386 1.3 66.6 1.0 F3 A:TF21386 2.1 69.8 1.0 F2 A:TF21386 2.2 66.4 1.0 C17 A:TF21386 2.4 69.1 1.0 O4 A:TF21386 2.7 66.0 1.0 C19 A:TF21386 2.9 70.3 1.0 O A:LEU160 3.0 50.6 1.0 CA A:LEU160 3.4 46.7 1.0 C A:LEU160 3.5 48.0 1.0 CB A:LEU160 3.6 45.0 1.0 CD2 A:LEU45 3.6 53.3 1.0 CD1 A:LEU45 3.7 55.5 1.0 C15 A:TF21386 3.7 71.0 1.0 CD2 A:LEU160 4.0 42.9 1.0 CB A:GLN163 4.0 54.4 1.0 CG A:LEU45 4.0 57.9 1.0 N A:HIS164 4.3 59.0 1.0 N2 A:TF21386 4.3 72.9 1.0 CG A:LEU160 4.4 46.9 1.0 CB A:HIS164 4.4 66.0 1.0 OG A:SER41 4.5 62.1 1.0 O3 A:TF21386 4.6 72.4 1.0 N A:ILE161 4.7 45.2 1.0 CA A:HIS164 4.8 62.5 1.0 N A:LEU160 4.8 43.4 1.0 C A:GLN163 4.8 57.1 1.0 CD1 A:LEU160 4.9 41.0 1.0 CA A:GLN163 5.0 55.0 1.0 CE2 A:PHE28 5.0 50.5 1.0

Fluorine binding site 2 out of 3 in the Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands within 5.0Å range: probe atom residue distance (Å) B Occ A:F1386 b:66.4 occ:1.00 F2 A:TF21386 0.0 66.4 1.0 C18 A:TF21386 1.3 66.6 1.0 F3 A:TF21386 2.1 69.8 1.0 F1 A:TF21386 2.2 65.0 1.0 C17 A:TF21386 2.4 69.1 1.0 O4 A:TF21386 2.8 66.0 1.0 N2 A:TF21386 2.8 72.9 1.0 C15 A:TF21386 2.9 71.0 1.0 CE2 A:PHE44 3.3 55.1 1.0 CD2 A:PHE44 3.5 53.9 1.0 CD2 A:LEU45 3.7 53.3 1.0 C19 A:TF21386 3.8 70.3 1.0 C8 A:TF21386 3.8 78.7 1.0 CD2 A:LEU160 3.9 42.9 1.0 O3 A:TF21386 4.0 72.4 1.0 CG A:LEU45 4.2 57.9 1.0 CB A:LEU160 4.5 45.0 1.0 CD1 A:LEU23 4.6 52.0 1.0 CZ A:PHE44 4.6 58.8 1.0 C4 A:TF21386 4.6 80.7 1.0 C9 A:TF21386 4.6 80.6 1.0 CE2 A:PHE28 4.6 50.5 1.0 CG A:LEU160 4.6 46.9 1.0 CD1 A:LEU45 4.6 55.5 1.0 C5 A:TF21386 4.7 80.2 1.0 CD1 A:LEU160 4.7 41.0 1.0 OG A:SER41 4.8 62.1 1.0 CA A:LEU160 4.8 46.7 1.0 CG A:PHE44 4.9 55.6 1.0

Fluorine binding site 3 out of 3 in the Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands within 5.0Å range: probe atom residue distance (Å) B Occ A:F1386 b:69.8 occ:1.00 F3 A:TF21386 0.0 69.8 1.0 C18 A:TF21386 1.3 66.6 1.0 F2 A:TF21386 2.1 66.4 1.0 F1 A:TF21386 2.1 65.0 1.0 C17 A:TF21386 2.4 69.1 1.0 C15 A:TF21386 2.9 71.0 1.0 CE2 A:PHE28 2.9 50.5 1.0 C19 A:TF21386 3.0 70.3 1.0 O3 A:TF21386 3.4 72.4 1.0 CD2 A:LEU160 3.4 42.9 1.0 CD2 A:PHE28 3.4 54.0 1.0 O4 A:TF21386 3.5 66.0 1.0 N2 A:TF21386 3.7 72.9 1.0 CB A:GLN163 3.8 54.4 1.0 CA A:LEU160 4.0 46.7 1.0 CZ A:PHE28 4.1 51.7 1.0 CG A:GLN163 4.2 54.1 1.0 CB A:LEU160 4.3 45.0 1.0 O A:LEU160 4.3 50.6 1.0 CG A:LEU160 4.5 46.9 1.0 O A:HOH2013 4.5 45.5 1.0 C A:LEU160 4.7 48.0 1.0 C8 A:TF21386 4.7 78.7 1.0 CG A:PHE28 4.8 55.8 1.0 N A:LEU160 4.9 43.4 1.0 CD1 A:LEU23 5.0 52.0 1.0 C5 A:TF21386 5.0 80.2 1.0

T.R.Knoechel, A.D.Tucker, C.M.Robinson, C.Phillips, W.Taylor, P.J.Bungay, S.A.Kasten, T.E.Roche, D.G.Brown. Regulatory Roles of the N-Terminal Domain Based on Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands. Biochemistry V. 45 402 2006.
ISSN: ISSN 0006-2960
PubMed: 16401071
DOI: 10.1021/BI051402S