Fluorine in PDB 2dux: Crystal Structure of Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1)

All present enzymatic activity of Crystal Structure of Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1):
1.1.1.21;

The structure of Crystal Structure of Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1), PDB code: 2dux was solved by H.Steuber, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.400, 67.000, 47.200, 90.00, 92.80, 90.00
R / Rfree (%)	16.3 / 22.7

The binding sites of Fluorine atom in the Crystal Structure of Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1) (pdb code 2dux). 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 Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1), PDB code: 2dux:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1)


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 Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1) within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:11.0 occ:1.00 F1 A:ZST600 0.0 11.0 1.0 C19 A:ZST600 1.3 12.0 1.0 F3 A:ZST600 2.1 15.2 1.0 F2 A:ZST600 2.1 14.1 1.0 C15 A:ZST600 2.3 7.3 1.0 C14 A:ZST600 2.7 6.0 1.0 CE3 A:TRP111 3.2 10.5 1.0 OG1 A:THR113 3.3 9.6 1.0 CG2 A:THR113 3.4 15.2 1.0 C16 A:ZST600 3.4 9.1 1.0 CD A:PRO310 3.4 15.3 1.0 CZ3 A:TRP111 3.9 6.5 1.0 CB A:THR113 3.9 6.9 1.0 CD2 A:TRP111 3.9 7.2 1.0 CG A:PRO310 4.0 13.1 1.0 C13 A:ZST600 4.0 12.1 1.0 CB A:TRP111 4.0 8.5 1.0 CD A:PRO112 4.2 6.0 1.0 CG A:TRP111 4.3 2.8 1.0 CG A:PRO112 4.5 6.9 1.0 C12 A:ZST600 4.5 8.3 1.0 CD1 A:TYR309 4.6 15.1 1.0 N A:THR113 4.6 13.7 1.0 C11 A:ZST600 4.7 6.7 1.0 N A:PRO310 4.8 9.6 1.0 CA A:TYR309 4.8 8.7 1.0 N A:PRO112 4.8 5.4 1.0 CA A:THR113 4.9 8.3 1.0 O A:ASP308 5.0 6.2 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1)


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 Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1) within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:14.1 occ:1.00 F2 A:ZST600 0.0 14.1 1.0 C19 A:ZST600 1.3 12.0 1.0 F1 A:ZST600 2.1 11.0 1.0 F3 A:ZST600 2.2 15.2 1.0 C15 A:ZST600 2.4 7.3 1.0 C14 A:ZST600 3.0 6.0 1.0 CB A:CYS303 3.1 15.6 1.0 CG2 A:THR113 3.4 15.2 1.0 C16 A:ZST600 3.4 9.1 1.0 CD1 A:TYR309 3.6 15.1 1.0 OG1 A:THR113 3.7 9.6 1.0 O A:CYS303 3.8 13.3 1.0 SG A:CYS303 4.0 16.4 1.0 CB A:THR113 4.0 6.9 1.0 CE1 A:TYR309 4.2 24.8 1.0 C A:CYS303 4.3 10.7 1.0 CD A:PRO310 4.3 15.3 1.0 C13 A:ZST600 4.3 12.1 1.0 CA A:CYS303 4.3 14.1 1.0 CA A:TYR309 4.5 8.7 1.0 C12 A:ZST600 4.6 8.3 1.0 CG A:TYR309 4.6 8.9 1.0 CB A:TYR309 4.7 9.4 1.0 CB A:HIS306 4.7 10.9 1.0 CE1 A:PHE115 4.8 11.7 1.0 C11 A:ZST600 4.9 6.7 1.0 CZ A:PHE115 4.9 11.3 1.0 CE3 A:TRP111 5.0 10.5 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1)


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 Human Aldose Reductase Complexed with Zopolrestat After 3 Days Soaking (3DAYS_SOAKED_1) within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:15.2 occ:1.00 F3 A:ZST600 0.0 15.2 1.0 C19 A:ZST600 1.3 12.0 1.0 F1 A:ZST600 2.1 11.0 1.0 F2 A:ZST600 2.2 14.1 1.0 C15 A:ZST600 2.3 7.3 1.0 C16 A:ZST600 2.6 9.1 1.0 CD1 A:TYR309 3.0 15.1 1.0 CE1 A:TYR309 3.1 24.8 1.0 CD A:PRO310 3.1 15.3 1.0 C14 A:ZST600 3.5 6.0 1.0 CG A:PRO310 3.8 13.1 1.0 CZ3 A:TRP111 3.9 6.5 1.0 CE3 A:TRP111 3.9 10.5 1.0 C12 A:ZST600 4.0 8.3 1.0 CG A:TYR309 4.1 8.9 1.0 CZ A:TYR309 4.3 19.2 1.0 CB A:CYS303 4.4 15.6 1.0 N A:PRO310 4.4 9.6 1.0 CA A:TYR309 4.5 8.7 1.0 CE2 A:PHE311 4.6 9.2 1.0 C13 A:ZST600 4.6 12.1 1.0 CB A:TYR309 4.7 9.4 1.0 CG2 A:THR113 4.8 15.2 1.0 CD2 A:PHE311 4.8 9.7 1.0 C11 A:ZST600 4.8 6.7 1.0 CH2 A:TRP111 4.9 6.0 1.0 CD2 A:TRP111 4.9 7.2 1.0 OH A:TYR309 5.0 18.0 1.0 O A:CYS303 5.0 13.3 1.0

H.Steuber, M.Zentgraf, C.Gerlach, C.A.Sotriffer, A.Heine, G.Klebe. Expect the Unexpected or Caveat For Drug Designers: Multiple Structure Determinations Using Aldose Reductase Crystals Treated Under Varying Soaking and Co-Crystallisation Conditions J.Mol.Biol. V. 363 174 2006.
ISSN: ISSN 0022-2836
PubMed: 16952371
DOI: 10.1016/J.JMB.2006.08.011