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Hydrolase PDB id
1wxz
Jmol
Contents
Protein chain
349 a.a. *
Ligands
FRL
Metals
_ZN
Waters ×138
* Residue conservation analysis
PDB id:
1wxz
Name: Hydrolase
Title: Crystal structure of adenosine deaminase ligated with a potent inhibitor
Structure: Adenosine deaminase. Chain: a. Synonym: adenosine aminohydrolase. Ec: 3.5.4.4
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: intestine
Resolution:
2.80Å     R-factor:   0.220     R-free:   0.223
Authors: T.Kinoshita
Key ref: T.Terasaka et al. (2005). Rational design of non-nucleoside, potent, and orally bioavailable adenosine deaminase inhibitors: predicting enzyme conformational change and metabolism. J Med Chem, 48, 4750-4753. PubMed id: 16033254 DOI: 10.1021/jm050413g
Date:
02-Feb-05     Release date:   16-Aug-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P56658  (ADA_BOVIN) -  Adenosine deaminase
Seq:
Struc: 		363 a.a.
349 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 15 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.5.4.4  - Adenosine deaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Adenosine + H2O = inosine + NH3
Adenosine
 + H(2)O
 =
inosine
Bound ligand (Het Group name = FRL)
matches with 40.00% similarity 		+ NH(3)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cell surface   10 terms 
  Biological process     cell adhesion   42 terms 
  Biochemical function     hydrolase activity     5 terms  

 

 
    Added reference    
 
 
DOI no: 10.1021/jm050413g J Med Chem 48:4750-4753 (2005)
PubMed id: 16033254  
 
 
Rational design of non-nucleoside, potent, and orally bioavailable adenosine deaminase inhibitors: predicting enzyme conformational change and metabolism.
T.Terasaka, K.Tsuji, T.Kato, I.Nakanishi, T.Kinoshita, Y.Kato, M.Kuno, T.Inoue, K.Tanaka, K.Nakamura.
 
  ABSTRACT  
 
From metabolic considerations and prediction of an inhibitor-induced conformational change, novel adenosine deaminase (ADA) inhibitors with improved activities and oral bioavailability have been developed on the basis of our originally designed non-nucleoside ADA inhibitors. They demonstrated in vivo efficacy in models of inflammation and lymphoma. Furthermore, X-ray crystal structure analysis has revealed a novel induced fit to ADA.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18602399 E.T.Larson, W.Deng, B.E.Krumm, A.Napuli, N.Mueller, W.C.Van Voorhis, F.S.Buckner, E.Fan, A.Lauricella, G.DeTitta, J.Luft, F.Zucker, W.G.Hol, C.L.Verlinde, and E.A.Merritt (2008).
Structures of substrate- and inhibitor-bound adenosine deaminase from a human malaria parasite show a dramatic conformational change and shed light on drug selectivity.
  J Mol Biol, 381, 975-988.
PDB codes: 2pgf 2pgr 2qvn
17379970 T.Kinoshita (2007).
[Application and development of structure-based drug design using X-ray analysis]
  Nippon Yakurigaku Zasshi, 129, 186-190.  
16580603 A.J.Orry, R.A.Abagyan, and C.N.Cavasotto (2006).
Structure-based development of target-specific compound libraries.
  Drug Discov Today, 11, 261-266.  
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.