3V35

Aldose reductase complexed with a nitro compound

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.183 
  • R-Value Work: 0.143 
  • R-Value Observed: 0.145 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history. 


Literature

Partial inhibition of aldose reductase by nitazoxanide and its molecular basis.

Zheng, X., Zhang, L., Chen, W., Chen, Y., Xie, W., Hu, X.

(2012) ChemMedChem 7: 1921-1923

  • DOI: https://doi.org/10.1002/cmdc.201200333
  • Primary Citation of Related Structures:  
    3V35, 3V36

  • PubMed Abstract: 

    A little is more than enough: Aldose reductase (AR) is a potential target in a wide range of diseases but its utility may be limited by the side effects caused by complete inhibition. Furthermore, known inhibitors of AR have suffered in clinical evaluation due to poor bioavailability. Here, the clinically used antiprotozoal drug nitazoxanide with proven bioavailability has been shown to partially inhibit AR, potentially circumventing the negatives effects of complete enzyme inhibition.

    • Organizational Affiliation: 

    School of Pharmaceutical Sciences, Sun Yat-sen University, Guangzhou 510006 (China).


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Aldose reductase336Homo sapiensMutation(s): 0 
Gene Names: AKR1B1, ALDR1
EC: 1.1.1.21 (PDB Primary Data), 1.1.1.372 (UniProt), 1.1.1.300 (UniProt), 1.1.1.54 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for P15121 (Homo sapiens)
Explore P15121 
Go to UniProtKB:  P15121
PHAROS:  P15121
GTEx:  ENSG00000085662 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15121
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 3 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
NAP
Query on NAP
Download Ideal Coordinates CCD File 
B [auth A]NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
C21 H28 N7 O17 P3
XJLXINKUBYWONI-NNYOXOHSSA-N
NTI
Query on NTI
Download Ideal Coordinates CCD File 
C [auth A]2-[(5-nitro-1,3-thiazol-2-yl)carbamoyl]phenyl acetate
C12 H9 N3 O5 S
YQNQNVDNTFHQSW-UHFFFAOYSA-N
DMF
Query on DMF
Download Ideal Coordinates CCD File 
D [auth A]
E [auth A]
F [auth A]
G [auth A]
H [auth A]
D [auth A],
E [auth A],
F [auth A],
G [auth A],
H [auth A],
I [auth A],
J [auth A],
K [auth A],
L [auth A],
M [auth A],
N [auth A],
O [auth A],
P [auth A],
Q [auth A],
R [auth A],
S [auth A],
T [auth A],
U [auth A],
V [auth A],
W [auth A],
X [auth A],
Y [auth A],
Z [auth A]
DIMETHYLFORMAMIDE
C3 H7 N O
ZMXDDKWLCZADIW-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
NTI BindingDB:  3V35 IC50: 8220 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.183 
  • R-Value Work: 0.143 
  • R-Value Observed: 0.145 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.927α = 90
b = 68.158β = 93.75
c = 48.934γ = 90
Software Package:
Software NamePurpose
CrysalisProdata collection
MOLREPphasing
PHENIXrefinement
CrysalisProdata reduction
SCALAdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-08-29
    Type: Initial release
  • Version 1.1: 2014-07-23
    Changes: Database references
  • Version 1.2: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Refinement description