Fluorine in PDB 4oz3: Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole

All present enzymatic activity of Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole:
4.6.1.1;

The structure of Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole, PDB code: 4oz3 was solved by M.Vinkovic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.22 / 1.70
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	99.257, 99.257, 97.635, 90.00, 90.00, 120.00
R / Rfree (%)	17.4 / 21.6

The binding sites of Fluorine atom in the Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole (pdb code 4oz3). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole, PDB code: 4oz3:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:30.7 occ:1.00 F1 A:1Z8501 0.0 30.7 1.0 C2 A:1Z8501 1.3 32.0 1.0 F3 A:1Z8501 2.1 43.0 1.0 F4 A:1Z8501 2.1 42.5 1.0 C5 A:1Z8501 2.3 37.4 1.0 N6 A:1Z8501 2.6 40.3 1.0 CA A:LEU166 3.2 18.3 1.0 N A:VAL167 3.3 14.6 1.0 NZ A:LYS95 3.5 32.5 1.0 C10 A:1Z8501 3.6 38.3 1.0 C A:LEU166 3.7 18.6 1.0 O A:PHE165 3.7 13.5 1.0 CE A:LYS95 3.8 28.0 1.0 N7 A:1Z8501 3.9 37.6 1.0 H22 A:1Z8501 4.0 40.8 1.0 CE1 A:PHE165 4.0 17.3 1.0 CD2 A:LEU166 4.0 32.6 1.0 N A:LEU166 4.1 14.9 1.0 CB A:LEU166 4.2 22.1 1.0 CG2 A:VAL167 4.2 16.8 1.0 C A:PHE165 4.3 14.1 1.0 CD1 A:PHE165 4.3 17.1 1.0 CD A:LYS95 4.4 32.9 1.0 O A:VAL335 4.4 21.8 1.0 C9 A:1Z8501 4.4 40.0 1.0 H8 A:1Z8501 4.4 38.8 1.0 C11 A:1Z8501 4.5 37.2 1.0 CA A:VAL167 4.5 14.1 1.0 C16 A:1Z8501 4.6 40.9 1.0 CZ A:PHE165 4.6 15.1 1.0 CG A:LEU166 4.7 28.7 1.0 O A:VAL167 4.7 19.0 1.0 CA A:PHE336 4.8 24.0 1.0 O A:LEU166 4.8 18.0 1.0 CB A:VAL167 4.8 16.8 1.0 CB A:PHE336 4.9 26.2 1.0 CB A:LYS95 4.9 16.5 1.0 CD2 A:LEU102 5.0 21.1 1.0

Fluorine binding site 2 out of 3 in the Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:43.0 occ:1.00 F3 A:1Z8501 0.0 43.0 1.0 C2 A:1Z8501 1.3 32.0 1.0 F1 A:1Z8501 2.1 30.7 1.0 F4 A:1Z8501 2.1 42.5 1.0 C5 A:1Z8501 2.3 37.4 1.0 H22 A:1Z8501 2.3 40.8 1.0 C16 A:1Z8501 3.2 40.9 1.0 C10 A:1Z8501 3.2 38.3 1.0 N6 A:1Z8501 3.3 40.3 1.0 CD2 A:LEU102 3.4 21.1 1.0 C11 A:1Z8501 3.6 37.2 1.0 CB A:LYS95 3.6 16.5 1.0 CE A:LYS95 4.0 28.0 1.0 CB A:LEU94 4.0 10.8 1.0 CG2 A:VAL167 4.1 16.8 1.0 CD A:LYS95 4.1 32.9 1.0 N7 A:1Z8501 4.3 37.6 1.0 C9 A:1Z8501 4.3 40.0 1.0 C15 A:1Z8501 4.3 41.4 1.0 CE1 A:PHE165 4.3 17.3 1.0 CD1 A:LEU94 4.5 13.6 1.0 NZ A:LYS95 4.5 32.5 1.0 H21 A:1Z8501 4.5 41.0 1.0 CG A:LYS95 4.5 29.6 1.0 CG A:LEU102 4.5 17.2 1.0 N A:VAL167 4.6 14.6 1.0 CB A:LEU102 4.6 13.1 1.0 N A:LYS95 4.7 12.5 1.0 CZ A:PHE165 4.7 15.1 1.0 C A:LEU94 4.8 13.7 1.0 CA A:LYS95 4.8 13.4 1.0 CG A:LEU94 4.9 12.7 1.0 H8 A:1Z8501 5.0 38.8 1.0 C12 A:1Z8501 5.0 43.8 1.0

Fluorine binding site 3 out of 3 in the Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human Solac Complexed with 4-Phenyl-3-(Trifluoromethyl)-1H-Pyrazole within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:42.5 occ:1.00 F4 A:1Z8501 0.0 42.5 1.0 C2 A:1Z8501 1.3 32.0 1.0 F1 A:1Z8501 2.1 30.7 1.0 F3 A:1Z8501 2.1 43.0 1.0 C5 A:1Z8501 2.3 37.4 1.0 H22 A:1Z8501 2.8 40.8 1.0 CD A:LYS95 2.9 32.9 1.0 CE A:LYS95 3.0 28.0 1.0 C10 A:1Z8501 3.0 38.3 1.0 NZ A:LYS95 3.1 32.5 1.0 C16 A:1Z8501 3.2 40.9 1.0 C11 A:1Z8501 3.3 37.2 1.0 N6 A:1Z8501 3.4 40.3 1.0 O A:VAL335 3.4 21.8 1.0 CB A:PHE336 3.6 26.2 1.0 CB A:LYS95 3.6 16.5 1.0 CG A:LYS95 3.8 29.6 1.0 CA A:PHE336 4.1 24.0 1.0 C15 A:1Z8501 4.2 41.4 1.0 C9 A:1Z8501 4.2 40.0 1.0 N7 A:1Z8501 4.4 37.6 1.0 C12 A:1Z8501 4.4 43.8 1.0 C A:VAL335 4.5 22.6 1.0 H21 A:1Z8501 4.5 41.0 1.0 CD2 A:LEU166 4.6 32.6 1.0 O A:PHE165 4.7 13.5 1.0 N A:PHE336 4.7 21.0 1.0 H18 A:1Z8501 4.8 44.4 1.0 CG A:PHE336 4.9 28.5 1.0 CA A:LEU166 5.0 18.3 1.0

S.M.Saalau-Bethell, V.Berdini, A.Cleasby, M.Congreve, J.E.Coyle, V.Lock, C.W.Murray, M.A.O'brien, S.J.Rich, T.Sambrook, M.Vinkovic, J.R.Yon, H.Jhoti. Crystal Structure of Human Soluble Adenylate Cyclase Reveals A Distinct, Highly Flexible Allosteric Bicarbonate Binding Pocket. Chemmedchem V. 9 823 2014.
ISSN: ESSN 1860-7187
PubMed: 24616449
DOI: 10.1002/CMDC.201300480