Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:19724118rdf:typepubmed:Citationlld:pubmed
pubmed-article:19724118lifeskim:mentionsumls-concept:C1644263lld:lifeskim
pubmed-article:19724118lifeskim:mentionsumls-concept:C0014894lld:lifeskim
pubmed-article:19724118lifeskim:mentionsumls-concept:C0678594lld:lifeskim
pubmed-article:19724118lifeskim:mentionsumls-concept:C2742100lld:lifeskim
pubmed-article:19724118pubmed:issuePt 9lld:pubmed
pubmed-article:19724118pubmed:dateCreated2009-9-2lld:pubmed
pubmed-article:19724118pubmed:abstractTextThe crystal structure of the esterase EstA from the cold-adapted bacterium Pseudoalteromonas sp. 643A was determined in a covalently inhibited form at a resolution of 1.35 A. The enzyme has a typical SGNH hydrolase structure consisting of a single domain containing a five-stranded beta-sheet, with three helices at the convex side and two helices at the concave side of the sheet, and is ornamented with a couple of very short helices at the domain edges. The active site is located in a groove and contains the classic catalytic triad of Ser, His and Asp. In the structure of the crystal soaked in diethyl p-nitrophenyl phosphate (DNP), the catalytic serine is covalently connected to a phosphonate moiety that clearly has only one ethyl group. This is the only example in the Protein Data Bank of a DNP-inhibited enzyme with covalently bound monoethylphosphate.lld:pubmed
pubmed-article:19724118pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:languageenglld:pubmed
pubmed-article:19724118pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:citationSubsetIMlld:pubmed
pubmed-article:19724118pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:19724118pubmed:statusMEDLINElld:pubmed
pubmed-article:19724118pubmed:monthSeplld:pubmed
pubmed-article:19724118pubmed:issn1744-3091lld:pubmed
pubmed-article:19724118pubmed:authorpubmed-author:DauterZbignie...lld:pubmed
pubmed-article:19724118pubmed:authorpubmed-author:NowakElzbieta...lld:pubmed
pubmed-article:19724118pubmed:authorpubmed-author:KurJózefJlld:pubmed
pubmed-article:19724118pubmed:authorpubmed-author:Cie?li?skiHub...lld:pubmed
pubmed-article:19724118pubmed:authorpubmed-author:Brzuszkiewicz...lld:pubmed
pubmed-article:19724118pubmed:authorpubmed-author:D?ugo?eckaAnn...lld:pubmed
pubmed-article:19724118pubmed:authorpubmed-author:DauterMiros?a...lld:pubmed
pubmed-article:19724118pubmed:issnTypeElectroniclld:pubmed
pubmed-article:19724118pubmed:day1lld:pubmed
pubmed-article:19724118pubmed:volume65lld:pubmed
pubmed-article:19724118pubmed:ownerNLMlld:pubmed
pubmed-article:19724118pubmed:authorsCompleteYlld:pubmed
pubmed-article:19724118pubmed:pagination862-5lld:pubmed
pubmed-article:19724118pubmed:dateRevised2010-9-2lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:meshHeadingpubmed-meshheading:19724118...lld:pubmed
pubmed-article:19724118pubmed:year2009lld:pubmed
pubmed-article:19724118pubmed:articleTitleStructure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate.lld:pubmed
pubmed-article:19724118pubmed:affiliationSynchrotron Radiation Research Section, MCL, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA.lld:pubmed
pubmed-article:19724118pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19724118pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:19724118pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
pubmed-article:19724118pubmed:publicationTypeResearch Support, N.I.H., Intramurallld:pubmed
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:19724118lld:entrezgene