PDBsum entry 2alr

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protein links
Oxidoreductase PDB id
Protein chain
312 a.a. *
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Aldehyde reductase
Structure: Aldehyde reductase. Chain: a. Synonym: alr1. Ec:
Source: Homo sapiens. Human. Organism_taxid: 9606. Organ: kidney. Tissue: medulla, cortex
2.48Å     R-factor:   0.190    
Authors: O.El-Kabbani
Key ref:
O.El-Kabbani et al. (1994). Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr D Biol Crystallogr, 50, 859-868. PubMed id: 15299353 DOI: 10.1107/S0907444994005275
06-Sep-94     Release date:   20-Jun-96    
Supersedes: 1alr
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P14550  (AK1A1_HUMAN) -  Alcohol dehydrogenase [NADP(+)]
325 a.a.
312 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Alcohol dehydrogenase (NADP(+)).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An alcohol + NADP+ = an aldehyde + NADPH
+ NADP(+)
= aldehyde
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular space   4 terms 
  Biological process     oxidation-reduction process   6 terms 
  Biochemical function     electron carrier activity     5 terms  


DOI no: 10.1107/S0907444994005275 Acta Crystallogr D Biol Crystallogr 50:859-868 (1994)
PubMed id: 15299353  
Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.
O.El-Kabbani, N.C.Green, G.Lin, M.Carson, S.V.Narayana, K.M.Moore, T.G.Flynn, L.J.DeLucas.
The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 A resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 A resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.
  Selected figure(s)  
Figure 3.
Fig. 3. Axcraee temperatture factor ~i :\~) per residue. computed for main-ch'ain (me)and side-chain i_ltoI]ls including C, (so): (a) for the t~vo molecule,,, of porcine ~ddchx de reductase: (F) for the human aldehxde reductase molecule.
Figure 5.
Fig. 5. The two crystallo- graphically independent mol- ecules for porcine aldehyde reductase with the non-crystallo- graphic twofold axis vertically oriented. The two molecules are viewed down the crystallo- graphic a axis. Ribbon drawings were prepared by using the pro- grams described by Carson (1987).
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1994, 50, 859-868) copyright 1994.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18300247 J.G.Olsen, L.Pedersen, C.L.Christensen, O.Olsen, and A.Henriksen (2008).
Barley aldose reductase: structure, cofactor binding, and substrate recognition in the aldo/keto reductase 4C family.
  Proteins, 71, 1572-1581.
PDB codes: 2bgq 2bgs 2vdg
18407998 L.Di Costanzo, J.E.Drury, T.M.Penning, and D.W.Christianson (2008).
Crystal structure of human liver Delta4-3-ketosteroid 5beta-reductase (AKR1D1) and implications for substrate binding and catalysis.
  J Biol Chem, 283, 16830-16839.
PDB codes: 3bur 3buv 3bv7 3cmf 3cot
11839745 E.Kozma, E.Brown, E.M.Ellis, and A.J.Lapthorn (2002).
The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily.
  J Biol Chem, 277, 16285-16293.
PDB code: 1gve
10651037 Q.Ye, D.Hyndman, X.Li, T.G.Flynn, and Z.Jia (2000).
Crystal structure of CHO reductase, a member of the aldo-keto reductase superfamily.
  Proteins, 38, 41-48.
PDB code: 1c9w
8877699 M.Carson (1996).
Wavelets and molecular structure.
  J Comput Aided Mol Des, 10, 273-283.  
8913694 M.von Itzstein, and P.Colman (1996).
Design and synthesis of carbohydrate-based inhibitors of protein-carbohydrate interactions.
  Curr Opin Struct Biol, 6, 703-709.  
  8762144 S.Janecek (1996).
Invariant glycines and prolines flanking in loops the strand beta 2 of various (alpha/beta)8-barrel enzymes: a hidden homology?
  Protein Sci, 5, 1136-1143.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.