Adenosine deaminase

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== 3D Structures of adenosine deaminase ==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*Adenosine deaminase
 
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**[[1vfl]] – bADA + Zn - bovine<BR />
 
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**[[3iar]] – hADA + Ni - human<BR />
 
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**[[3lgd]] – hADA2 + Zn<BR />
 
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**[[3mvt]] – mADA – mouse<BR />
 
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**[[3mvi]] – mADA + Zn<BR />
 
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**[[3ou8]] – PaADA + Zn – ''Pseudomonas aeruginosa''<BR />
 
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**[[2amx]] – ADA + Co – ''Plasmodium yoeli''<BR />
 
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**[[4gxw]] – ADA + Zn – ''Burkholderia ambifaria'' <BR />
 
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*Adenosine deaminase complex with nucleotide
 
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**[[1add]] – mADA + Zn + deaza-adenosine <BR />
 
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**[[3km8]] – mADA (mutant) + Zn + deaza-adenosine <BR />
 
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**[[2ada]] – mADA + Zn + transition state analog<BR />
 
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**[[1fkw]], [[1fkx]], [[1uio]], [[1uip]] – mADA (mutant) + Zn + adenosine analog<BR />
 
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**[[1a4m]] – mADA + Zn + adenosine analog<BR />
 
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**[[1krm]] – bADA + Zn + adenosine analog <BR />
 
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**[[2pgf]] – PvADA + Zn + adenosine – ''Plasmodium vivax''<BR />
 
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**[[2pgr]] – PvADA + Zn + adenosine analog<BR />
 
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**[[2qvn]] – PvADA + guanosine <BR />
 
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**[[3pan]] – PaADA + Zn + hypoxanthine <BR />
 
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**[[3pao]] – PaADA + Zn + adenine <BR />
 
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**[[3rys]] – ADA + Zn + adenine – ''Arthrobacter aurescens''<BR />
 
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*Adenosine deaminase complex with inhibitor
 
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**[[1a4l]] – mADA + Zn + inhibitor<BR />
 
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**[[1ndv]], [[1ndw]], [[1ndy]], [[1ndz]], [[1o5r]], [[1qxl]], [[1uml]], [[1v79]], [[1v7a]], [[1wxy]], [[1wxz]], [[2e1w]], [[2z7g]] – bADA + Zn + inhibitor<BR />
 
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**[[3ewc]] – PvADA + Zn + inhibitor<BR />
 
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**[[3ewd]] – PvADA (mutant) + Zn + inhibitor<BR />
 
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**[[3pbm]] – PaADA + Zn + chloropurine <BR />
 
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**[[3lgg]] – hADA2 + Zn + coformycin<BR />
 
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**[[6n9m]] – ADA + Zn + pentostatin – ''Salmonella typhimurium''<BR />
 
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**[[6n91]] – ADA + Zn + pentostatin – ''Vibrio cholerae''<BR />
 
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*Adenosine deaminase complex with protein
 
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**[[1w1i]] – bADA + Zn + dipeptidyl peptidase IV<BR />
 
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**[[2bgn]] – bADA + Zn + dipeptidyl peptidase IV + HIV1 TAT protein peptide<BR />
 
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*Double-stranded RNA-specific adenosine deaminase; domains – Zα 125-201; Zβ 294-366; 3rd RNA-binding 708-801; catalytic 299-729
 
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**[[1xmk]] – hADA Zα domain <br />
 
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**[[1qgp]] – hADA Zα domain - NMR<br />
 
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**[[2l54]] – hADA Zα domain (mutant) - NMR<br />
 
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**[[2acj]], [[1qbj]], [[2gxb]], [[3f21]], [[3f22]], [[3f23]], [[3irq]], [[3irr]], [[5zu1]], [[5zuo]], [[5zup]] – hADA Zα domain + DNA<br />
 
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**[[2mdr]] – hADA 3rd RNA-binding domain - NMR<br />
 
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**[[1zy7]] – hADA catalytic domain + inositol hexakisphosphate<br />
 
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**[[6d06]], [[5hp2]], [[5hp3]], [[5ed1]], [[5ed2]] – hADA catalytic domain + RNA<br />
 
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**[[2b7t]], [[2b7v]] – rADA 1st RNA-binding domain – rat<br />
 
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**[[2l3c]], [[2l3j]] – rADA 1st RNA-binding domain + RNA – NMR<br />
 
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**[[2l2k]] – mADA residues 230-301 + RNA – NMR<br />
 
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**[[2ljh]] – ADA DRBM domain – ''Drosophila melanogaster'' – NMR<br />
 
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*tRNA-specific adenosine deaminase
 
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**[[1z3a]] – ADA – Escherichia coli<br />
 
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**[[2b3j]] – ADA + Zn + tRNA stem-loop – ''Stapphylococcus aureus''<BR />
 
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**[[1wwr]] – ADA – ''Aquifex aeolicus''<br />
 
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**[[2nx8]] – ADA (mutant) + Zn – ''Streptococcus pyogenes''<br />
 
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**[[3dh1]] – hADA subunit ADAT2<br />
 
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}}
 
==References ==
==References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 10:42, 28 February 2019

Structure of adenosine deaminase complex with Zn+2 (grey), acetonitrile and adenosine (stick figure) (PDB entry 2pgf)

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References

  1. Wilson DK, Rudolph FB, Quiocho FA. Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations. Science. 1991 May 31;252(5010):1278-84. PMID:1925539
  2. Larson ET, Deng W, Krumm BE, Napuli A, Mueller N, Van Voorhis WC, Buckner FS, Fan E, Lauricella A, DeTitta G, Luft J, Zucker F, Hol WG, Verlinde CL, Merritt EA. 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. 2008 Sep 12;381(4):975-88. Epub 2008 Jun 24. PMID:18602399 doi:http://dx.doi.org/10.1016/j.jmb.2008.06.048

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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