Fluorine in PDB 4i5x: Crystal Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid

The structure of Crystal Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid, PDB code: 4i5x was solved by L.Zhang, X.Zheng, S.Chen, J.Zhai, H.Zhang, Y.Zhao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.61 / 2.10
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	89.402, 89.402, 77.874, 90.00, 90.00, 120.00
R / Rfree (%)	19.6 / 25.7

The binding sites of Fluorine atom in the Crystal Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid (pdb code 4i5x). 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 Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid, PDB code: 4i5x:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid


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 AKR1B10 Complexed with Nadp+ and Flufenamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:54.6 occ:1.00 F1 A:FLF401 0.0 54.6 1.0 C7' A:FLF401 1.3 57.7 1.0 F3 A:FLF401 2.1 54.0 1.0 F2 A:FLF401 2.2 51.5 1.0 C3' A:FLF401 2.4 49.6 1.0 C4' A:FLF401 2.8 43.3 1.0 CD A:LYS22 3.1 50.6 1.0 CB A:LYS22 3.3 47.4 1.0 O A:HOH658 3.4 40.6 1.0 C2' A:FLF401 3.6 50.6 1.0 CG A:LYS22 3.8 53.5 1.0 C5' A:FLF401 4.1 42.1 1.0 CE A:LYS22 4.4 45.0 1.0 CA A:LYS22 4.6 49.2 1.0 NE1 A:TRP21 4.7 42.8 1.0 NZ A:LYS22 4.7 35.6 1.0 C1' A:FLF401 4.8 46.5 1.0 N A:LYS22 4.8 46.3 1.0 C6' A:FLF401 5.0 39.9 1.0 CE2 A:TRP21 5.0 49.5 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:51.5 occ:1.00 F2 A:FLF401 0.0 51.5 1.0 C7' A:FLF401 1.4 57.7 1.0 F1 A:FLF401 2.2 54.6 1.0 F3 A:FLF401 2.2 54.0 1.0 C3' A:FLF401 2.4 49.6 1.0 C2' A:FLF401 3.1 50.6 1.0 C4' A:FLF401 3.3 43.3 1.0 CZ2 A:TRP21 3.7 46.3 1.0 CG A:PRO219 3.8 27.0 1.0 NE1 A:TRP21 3.8 42.8 1.0 CE2 A:TRP21 3.9 49.5 1.0 CD A:PRO219 4.0 28.5 1.0 O A:HOH561 4.4 36.1 1.0 C1' A:FLF401 4.4 46.5 1.0 C5' A:FLF401 4.6 42.1 1.0 CH2 A:TRP21 4.6 46.4 1.0 CD1 A:TRP21 4.9 49.4 1.0 CB A:LYS22 4.9 47.4 1.0 C6' A:FLF401 5.0 39.9 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of AKR1B10 Complexed with Nadp+ and Flufenamic Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:54.0 occ:1.00 F3 A:FLF401 0.0 54.0 1.0 C7' A:FLF401 1.3 57.7 1.0 F1 A:FLF401 2.1 54.6 1.0 F2 A:FLF401 2.2 51.5 1.0 C3' A:FLF401 2.4 49.6 1.0 NE1 A:TRP21 2.8 42.8 1.0 C2' A:FLF401 2.8 50.6 1.0 CE2 A:TRP21 3.0 49.5 1.0 CZ2 A:TRP21 3.4 46.3 1.0 CD1 A:TRP21 3.4 49.4 1.0 CB A:LYS22 3.4 47.4 1.0 C4' A:FLF401 3.5 43.3 1.0 CD2 A:TRP21 3.6 51.8 1.0 N A:LYS22 3.8 46.3 1.0 CG A:TRP21 3.8 46.5 1.0 C1' A:FLF401 4.2 46.5 1.0 CA A:LYS22 4.2 49.2 1.0 CH2 A:TRP21 4.2 46.4 1.0 CE1 A:TYR49 4.3 42.7 1.0 CE3 A:TRP21 4.4 35.0 1.0 CD1 A:TYR49 4.4 37.2 1.0 CG A:LYS22 4.6 53.5 1.0 CD A:LYS22 4.6 50.6 1.0 O A:HOH561 4.6 36.1 1.0 C5' A:FLF401 4.7 42.1 1.0 CZ3 A:TRP21 4.7 37.4 1.0 O A:LYS22 4.7 49.3 1.0 C A:TRP21 4.8 46.8 1.0 O A:HOH658 4.8 40.6 1.0 C6' A:FLF401 4.9 39.9 1.0 C A:LYS22 5.0 57.5 1.0 CB A:TRP21 5.0 32.5 1.0

L.Zhang, H.Zhang, Y.Zhao, Z.Li, S.Chen, J.Zhai, Y.Chen, W.Xie, Z.Wang, Q.Li, X.Zheng, X.Hu. Inhibitor Selectivity Between Aldo-Keto Reductase Superfamily Members AKR1B10 and AKR1B1: Role of TRP112 (TRP111) Febs Lett. V. 587 3681 2013.
ISSN: ISSN 0014-5793
PubMed: 24100137
DOI: 10.1016/J.FEBSLET.2013.09.031