Fluorine in PDB 5ouk: Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 41

All present enzymatic activity of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 41:
1.1.1.21;

The structure of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 41, PDB code: 5ouk was solved by A.Cousido-Siah, F.X.Ruiz, A.Mitschler, K.Metwally, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.14 / 0.96
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	40.286, 47.076, 47.304, 76.34, 67.52, 76.76
R / Rfree (%)	13.5 / 14.9

The binding sites of Fluorine atom in the Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 41 (pdb code 5ouk). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 41, PDB code: 5ouk:

Fluorine binding site 1 out of 1 in the Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 41


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 41 within 5.0Å range: probe atom residue distance (Å) B Occ A:F402 b:17.9 occ:0.88 F27 A:AVT402 0.0 17.9 0.9 C5 A:AVT402 1.4 17.1 0.9 C6 A:AVT402 2.3 18.1 0.9 C3 A:AVT402 2.4 16.3 0.9 O A:HOH757 3.0 36.4 1.0 O A:VAL47 3.0 8.7 1.0 OE1 A:GLN49 3.5 24.6 1.0 C4 A:AVT402 3.6 17.9 0.9 CG2 A:VAL47 3.7 8.6 1.0 C1 A:AVT402 3.7 15.6 0.9 CD2 A:PHE121 3.7 16.9 1.0 O A:HOH739 4.1 21.9 1.0 C2 A:AVT402 4.1 16.8 0.9 C A:VAL47 4.2 7.2 1.0 CD A:GLN49 4.2 22.2 1.0 CE2 A:PHE121 4.3 17.7 1.0 CG A:GLN49 4.5 17.4 1.0 CB A:VAL47 4.7 7.3 1.0 O A:HOH843 4.7 44.8 1.0 CG A:PHE121 4.7 14.3 1.0 CA A:VAL47 4.7 7.3 1.0 O21 A:AVT402 4.8 12.1 0.9 CB A:PHE121 4.9 12.1 1.0 C7 A:AVT402 4.9 14.3 0.9 O A:HOH884 4.9 45.1 1.0

I.Crespo, J.Gimenez-Dejoz, S.Porte, A.Cousido-Siah, A.Mitschler, A.Podjarny, H.Pratsinis, D.Kletsas, X.Pares, F.X.Ruiz, K.Metwally, J.Farres. Design, Synthesis, Structure-Activity Relationships and X-Ray Structural Studies of Novel 1-Oxopyrimido[4,5-C]Quinoline-2-Acetic Acid Derivatives As Selective and Potent Inhibitors of Human Aldose Reductase. Eur J Med Chem V. 152 160 2018.
ISSN: ISSN 1768-3254
PubMed: 29705708
DOI: 10.1016/J.EJMECH.2018.04.015