1EKO: Pig Aldose Reductase Complexed With Idd384 Inhibitor

Citation:
Abstract
The crystallographic structure of the complex between human aldose reductase (AR2) and one of its inhibitors, IDD384, has been solved at 1.7 A resolution from crystals obtained at pH 5.0. This structure shows that the binding of the inhibitor's hydrophilic head to the catalytic residues Tyr48 and His110 differs from that found previously with porcine AR2. The difference is attributed to a change in the protonation state of the inhibitor (pK(a) = 4.52) when soaked with crystals of human (at pH 5.0) or pig lens AR2 (at pH 6.2). This work demonstrates how strongly the detailed binding of the inhibitor's polar head depends on its protonation state.
PDB ID: 1EKODownload
MMDB ID: 13500
PDB Deposition Date: 2000/3/9
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 1EKO: monomeric; determined by author
Molecular Components in 1EKO
Label Count Molecule
Protein (1 molecule)
1
Aldose Reductase(Gene symbol: AKR1B1)
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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