Fluorine in PDB 2i16: Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K

All present enzymatic activity of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K:
1.1.1.21;

The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K, PDB code: 2i16 was solved by T.Petrova, S.Ginell, A.Mitshler, I.Hasemann, T.Schneider, A.Cousido, V.Y.Lunin, A.Joachimiak, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 0.81
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.173, 66.671, 47.297, 90.00, 92.26, 90.00
R / Rfree (%)	8.6 / 9.7

The structure of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K also contains other interesting chemical elements:

Bromine

(Br)

1 atom

The binding sites of Fluorine atom in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K (pdb code 2i16). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K, PDB code: 2i16:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K within 5.0Å range: probe atom residue distance (Å) B Occ A:F321 b:3.2 occ:1.00 F9 A:LDT321 0.0 3.2 1.0 C5 A:LDT321 1.4 2.7 1.0 C2 A:LDT321 2.3 2.5 1.0 C6 A:LDT321 2.3 2.9 1.0 O A:VAL48 3.0 2.1 1.0 O A:HOH485 3.3 6.3 1.0 O A:HOH484 3.5 3.8 1.0 C A:VAL48 3.5 1.7 1.0 CD1 A:TYR49 3.6 1.9 1.0 O A:HOH965 3.6 6.6 0.5 CG1 A:VAL48 3.6 1.9 1.0 C3 A:LDT321 3.6 2.8 1.0 C4 A:LDT321 3.6 2.3 1.0 O A:HOH972 3.8 5.8 0.7 CG2 A:VAL48 3.9 2.1 1.0 CA A:TYR49 3.9 1.9 1.0 N A:TYR49 3.9 1.7 1.0 NE1 A:TRP21 4.0 2.9 1.0 CD1 A:TRP21 4.0 2.6 1.0 C7 A:LDT321 4.1 2.6 1.0 CB A:VAL48 4.1 1.7 1.0 CE1 A:TYR49 4.2 1.8 1.0 CA A:VAL48 4.5 1.8 1.0 CG A:TYR49 4.6 1.8 1.0 O A:HOH606 4.7 4.8 1.0 O15 A:LDT321 4.7 2.6 1.0 CB A:TYR49 4.8 1.9 1.0 O A:HOH477 4.8 5.2 1.0 C A:TYR49 4.8 2.0 1.0

Fluorine binding site 2 out of 2 in the Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Aldose Reductase in Complex with Nadp+ and the Inhibitor IDD594 at Temperature of 15K within 5.0Å range: probe atom residue distance (Å) B Occ A:F321 b:3.5 occ:1.00 F14 A:LDT321 0.0 3.5 1.0 C27 A:LDT321 1.4 2.9 1.0 C24 A:LDT321 2.4 2.9 1.0 C28 A:LDT321 2.4 3.1 1.0 C13 A:LDT321 2.8 3.3 1.0 C A:ALA300 3.0 4.4 1.0 CA A:ALA300 3.0 4.4 1.0 CH2 A:TRP112 3.2 3.2 1.0 N A:ALA300 3.2 3.9 1.0 N A:LEU301 3.3 4.1 1.0 O A:ALA300 3.5 4.8 1.0 CB A:LEU301 3.5 4.1 1.0 C A:CYS299 3.6 4.0 0.5 C25 A:LDT321 3.6 2.8 1.0 C26 A:LDT321 3.6 2.8 1.0 CZ2 A:TRP112 3.6 3.3 1.0 C A:CYS299 3.7 2.6 0.5 O A:CYS299 3.7 4.2 0.5 CZ3 A:TRP112 3.7 2.9 1.0 O A:CYS299 4.0 4.7 0.5 CA A:LEU301 4.0 3.9 1.0 C29 A:LDT321 4.1 2.8 1.0 N17 A:LDT321 4.2 2.9 1.0 CA A:CYS299 4.3 3.7 0.5 CB A:CYS299 4.4 3.6 0.5 CE2 A:TRP112 4.4 2.8 1.0 OH A:TYR310 4.4 5.0 1.0 SG A:CYS299 4.5 2.9 0.5 CB A:ALA300 4.5 5.8 1.0 CE3 A:TRP112 4.5 2.5 1.0 CE2 A:PHE312 4.7 3.7 0.5 CE2 A:PHE312 4.7 4.8 0.5 CA A:CYS299 4.7 2.8 0.5 CE1 A:TYR310 4.8 4.3 1.0 CD2 A:TRP112 4.9 2.5 1.0 CG A:LEU301 4.9 4.6 1.0

T.Petrova, S.Ginell, A.Mitschler, I.Hazemann, T.Schneider, A.Cousido, V.Y.Lunin, A.Joachimiak, A.Podjarny. Ultrahigh-Resolution Study of Protein Atomic Displacement Parameters at Cryotemperatures Obtained with A Helium Cryostat. Acta Crystallogr.,Sect.D V. 62 1535 2006.
ISSN: ISSN 0907-4449
PubMed: 17139089
DOI: 10.1107/S0907444906041035