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Fluorine in PDB 5ouj: Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39

Enzymatic activity of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39

All present enzymatic activity of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39:
1.1.1.21;

Protein crystallography data

The structure of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39, PDB code: 5ouj 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) 28.90 / 0.96
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 40.050, 46.979, 47.283, 76.40, 67.57, 77.40
R / Rfree (%) 13 / 14.7

Other elements in 5ouj:

The structure of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39 (pdb code 5ouj). 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 39, PDB code: 5ouj:

Fluorine binding site 1 out of 1 in 5ouj

Go back to Fluorine Binding Sites List in 5ouj
Fluorine binding site 1 out of 1 in the Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39


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 39 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F402

b:44.2
occ:0.96
 F27 A:AW8402 0.0 44.2 1.0
C5 A:AW8402 1.4 43.6 1.0
C3 A:AW8402 2.4 41.4 1.0
C6 A:AW8402 2.4 44.1 1.0
O A:HOH673 2.4 17.5 0.5
O A:VAL47 2.7 8.3 1.0
O A:HOH750 2.7 14.6 0.4
O A:HOH815 3.4 20.4 1.0
OE1 A:GLN49 3.6 24.4 1.0
C1 A:AW8402 3.7 38.3 1.0
C4 A:AW8402 3.7 43.9 1.0
O A:HOH634 3.7 10.9 1.0
C A:VAL47 3.9 7.2 1.0
CA A:TYR48 4.0 7.5 1.0
C A:TYR48 4.2 7.8 1.0
O A:TYR48 4.2 9.0 1.0
C2 A:AW8402 4.2 42.4 1.0
O A:HOH750 4.2 15.3 0.6
CG A:GLN49 4.2 14.8 1.0
CD A:GLN49 4.3 21.1 1.0
N A:TYR48 4.4 6.8 1.0
O21 A:AW8402 4.5 17.2 1.0
NE1 A:TRP20 4.7 8.7 1.0
CD1 A:TRP20 4.7 8.1 1.0
CB A:GLN49 4.7 11.7 1.0
N A:GLN49 4.9 7.8 1.0
CG2 A:VAL47 4.9 9.1 1.0
C7 A:AW8402 4.9 30.2 1.0

Reference:

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
Page generated: Thu Aug 1 12:35:39 2024

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