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Fluorine in PDB 2iki: Human Aldose Reductase Complexed with Halogenated Idd-Type Inhibitor

Enzymatic activity of Human Aldose Reductase Complexed with Halogenated Idd-Type Inhibitor

All present enzymatic activity of Human Aldose Reductase Complexed with Halogenated Idd-Type Inhibitor:
1.1.1.21;

Protein crystallography data

The structure of Human Aldose Reductase Complexed with Halogenated Idd-Type Inhibitor, PDB code: 2iki was solved by H.Steuber, C.Koch, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.47
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.361, 66.802, 47.318, 90.00, 92.37, 90.00
R / Rfree (%) 14.8 / 18.1

Other elements in 2iki:

The structure of Human Aldose Reductase Complexed with Halogenated Idd-Type Inhibitor also contains other interesting chemical elements:

Bromine (Br) 1 atom
Chlorine (Cl) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Human Aldose Reductase Complexed with Halogenated Idd-Type Inhibitor (pdb code 2iki). 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 Human Aldose Reductase Complexed with Halogenated Idd-Type Inhibitor, PDB code: 2iki:

Fluorine binding site 1 out of 1 in 2iki

Go back to Fluorine Binding Sites List in 2iki
Fluorine binding site 1 out of 1 in the Human Aldose Reductase Complexed with Halogenated Idd-Type Inhibitor


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 Complexed with Halogenated Idd-Type Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F600

b:11.1
occ:1.00
 F9 A:388600 0.0 11.1 1.0
C7 A:388600 1.3 8.0 1.0
C2 A:388600 2.3 8.7 1.0
C6 A:388600 2.4 9.6 1.0
C1 A:388600 2.7 8.2 1.0
C A:ALA299 3.1 15.3 1.0
CA A:ALA299 3.1 13.2 1.0
N A:LEU300 3.2 12.3 1.0
CH2 A:TRP111 3.2 8.3 1.0
N A:ALA299 3.3 11.0 1.0
CB A:LEU300 3.6 13.3 1.0
C A:CYS298 3.6 14.0 1.0
C3 A:388600 3.6 9.6 1.0
C5 A:388600 3.6 9.4 1.0
CZ3 A:TRP111 3.7 11.4 1.0
O A:ALA299 3.7 21.6 1.0
CZ2 A:TRP111 3.7 11.4 1.0
O A:CYS298 3.7 13.5 1.0
CA A:LEU300 4.0 12.9 1.0
N10 A:388600 4.1 11.1 1.0
C4 A:388600 4.1 10.3 1.0
OH A:TYR309 4.2 14.7 1.0
CE3 A:TRP111 4.5 8.6 1.0
CE1 A:TYR309 4.5 9.9 1.0
CA A:CYS298 4.5 9.0 1.0
CE2 A:TRP111 4.5 10.2 1.0
CE2 A:PHE311 4.5 13.7 1.0
CB A:ALA299 4.6 12.6 1.0
CB A:CYS298 4.7 15.9 1.0
CZ A:TYR309 4.8 15.7 1.0
CG A:LEU300 4.9 12.1 1.0
CD2 A:TRP111 4.9 7.4 1.0

Reference:

H.Steuber, A.Heine, G.Klebe. Structural and Thermodynamic Study on Aldose Reductase: Nitro-Substituted Inhibitors with Strong Enthalpic Binding Contribution J.Mol.Biol. V. 368 618 2007.
ISSN: ISSN 0022-2836
PubMed: 17368668
DOI: 10.1016/J.JMB.2006.12.004
Page generated: Wed Jul 31 14:54:33 2024

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