Fluorine in PDB 2bu5: 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: 2bu5 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 / 2.35
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	108.074, 108.074, 84.385, 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 2bu5). 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: 2bu5:
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:73.4 occ:1.00 F1 A:TF11386 0.0 73.4 1.0 C8 A:TF11386 1.3 71.8 1.0 F2 A:TF11386 2.1 71.8 1.0 F3 A:TF11386 2.1 72.3 1.0 C4 A:TF11386 2.4 71.5 1.0 C9 A:TF11386 2.8 72.6 1.0 C1 A:TF11386 3.1 67.6 1.0 CE2 A:PHE28 3.2 54.0 1.0 CB A:GLN163 3.3 57.4 1.0 O1 A:TF11386 3.5 67.3 1.0 O2 A:TF11386 3.6 71.3 1.0 CD2 A:LEU160 3.6 47.4 1.0 CD2 A:PHE28 3.8 54.2 1.0 CA A:LEU160 3.8 47.9 1.0 CG A:GLN163 3.8 57.3 1.0 O A:LEU160 3.9 48.2 1.0 N1 A:TF11386 4.0 66.0 1.0 CZ A:PHE28 4.3 53.4 1.0 CB A:LEU160 4.3 47.0 1.0 C A:LEU160 4.3 49.2 1.0 C3 A:TF11386 4.5 65.6 1.0 CG A:LEU160 4.6 48.5 1.0 CD1 A:LEU23 4.6 49.1 1.0 CA A:GLN163 4.7 58.3 1.0 N A:LEU160 4.8 45.4 1.0 O A:MET159 4.8 48.1 1.0 N A:HIS164 5.0 61.2 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:71.8 occ:1.00 F2 A:TF11386 0.0 71.8 1.0 C8 A:TF11386 1.3 71.8 1.0 F1 A:TF11386 2.1 73.4 1.0 F3 A:TF11386 2.1 72.3 1.0 C4 A:TF11386 2.4 71.5 1.0 O2 A:TF11386 2.8 71.3 1.0 C9 A:TF11386 2.9 72.6 1.0 O A:LEU160 3.3 48.2 1.0 CD2 A:LEU45 3.3 56.5 1.0 CD1 A:LEU45 3.6 56.2 1.0 CG A:LEU45 3.8 59.1 1.0 CA A:LEU160 3.8 47.9 1.0 C A:LEU160 3.8 49.2 1.0 CB A:LEU160 3.8 47.0 1.0 C1 A:TF11386 3.8 67.6 1.0 CD2 A:LEU160 4.1 47.4 1.0 OG A:SER41 4.2 64.0 1.0 CB A:GLN163 4.3 57.4 1.0 N A:HIS164 4.5 61.2 1.0 CG A:LEU160 4.5 48.5 1.0 CB A:HIS164 4.5 65.3 1.0 N1 A:TF11386 4.5 66.0 1.0 C3 A:TF11386 4.6 65.6 1.0 O1 A:TF11386 4.6 67.3 1.0 CD1 A:LEU160 4.9 46.8 1.0 CA A:HIS164 4.9 63.4 1.0 CD2 A:PHE44 4.9 65.7 1.0 CE2 A:PHE44 5.0 65.4 1.0 N A:ILE161 5.0 48.4 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:72.3 occ:1.00 F3 A:TF11386 0.0 72.3 1.0 C8 A:TF11386 1.3 71.8 1.0 F1 A:TF11386 2.1 73.4 1.0 F2 A:TF11386 2.1 71.8 1.0 C4 A:TF11386 2.5 71.5 1.0 C3 A:TF11386 2.9 65.6 1.0 O2 A:TF11386 3.0 71.3 1.0 C1 A:TF11386 3.1 67.6 1.0 N1 A:TF11386 3.2 66.0 1.0 CD2 A:LEU160 3.5 47.4 1.0 CE2 A:PHE44 3.5 65.4 1.0 CD1 A:LEU23 3.6 49.1 1.0 C9 A:TF11386 3.7 72.6 1.0 CD2 A:PHE44 3.9 65.7 1.0 CD2 A:LEU45 4.0 56.5 1.0 O1 A:TF11386 4.1 67.3 1.0 CE2 A:PHE28 4.2 54.0 1.0 CG A:LEU160 4.3 48.5 1.0 CB A:LEU160 4.4 47.0 1.0 CD1 A:LEU160 4.4 46.8 1.0 C7 A:TF11386 4.4 66.5 1.0 C2 A:TF11386 4.5 64.3 1.0 CA A:LEU160 4.6 47.9 1.0 C6 A:TF11386 4.6 60.7 1.0 CZ A:PHE44 4.7 66.6 1.0 CG A:LEU45 4.7 59.1 1.0 CD2 A:PHE28 5.0 54.2 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