pubmed-article:19724118 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19724118 | lifeskim:mentions | umls-concept:C1644263 | lld:lifeskim |
pubmed-article:19724118 | lifeskim:mentions | umls-concept:C0014894 | lld:lifeskim |
pubmed-article:19724118 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:19724118 | lifeskim:mentions | umls-concept:C2742100 | lld:lifeskim |
pubmed-article:19724118 | pubmed:issue | Pt 9 | lld:pubmed |
pubmed-article:19724118 | pubmed:dateCreated | 2009-9-2 | lld:pubmed |
pubmed-article:19724118 | pubmed:abstractText | The 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:19724118 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:language | eng | lld:pubmed |
pubmed-article:19724118 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19724118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19724118 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19724118 | pubmed:month | Sep | lld:pubmed |
pubmed-article:19724118 | pubmed:issn | 1744-3091 | lld:pubmed |
pubmed-article:19724118 | pubmed:author | pubmed-author:DauterZbignie... | lld:pubmed |
pubmed-article:19724118 | pubmed:author | pubmed-author:NowakElzbieta... | lld:pubmed |
pubmed-article:19724118 | pubmed:author | pubmed-author:KurJózefJ | lld:pubmed |
pubmed-article:19724118 | pubmed:author | pubmed-author:Cie?li?skiHub... | lld:pubmed |
pubmed-article:19724118 | pubmed:author | pubmed-author:Brzuszkiewicz... | lld:pubmed |
pubmed-article:19724118 | pubmed:author | pubmed-author:D?ugo?eckaAnn... | lld:pubmed |
pubmed-article:19724118 | pubmed:author | pubmed-author:DauterMiros?a... | lld:pubmed |
pubmed-article:19724118 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19724118 | pubmed:day | 1 | lld:pubmed |
pubmed-article:19724118 | pubmed:volume | 65 | lld:pubmed |
pubmed-article:19724118 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19724118 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19724118 | pubmed:pagination | 862-5 | lld:pubmed |
pubmed-article:19724118 | pubmed:dateRevised | 2010-9-2 | lld:pubmed |
pubmed-article:19724118 | pubmed:meshHeading | pubmed-meshheading:19724118... | lld:pubmed |
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pubmed-article:19724118 | pubmed:meshHeading | pubmed-meshheading:19724118... | lld:pubmed |
pubmed-article:19724118 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19724118 | pubmed:articleTitle | Structure of EstA esterase from psychrotrophic Pseudoalteromonas sp. 643A covalently inhibited by monoethylphosphonate. | lld:pubmed |
pubmed-article:19724118 | pubmed:affiliation | Synchrotron Radiation Research Section, MCL, National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA. | lld:pubmed |
pubmed-article:19724118 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19724118 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:19724118 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
pubmed-article:19724118 | pubmed:publicationType | Research Support, N.I.H., Intramural | lld:pubmed |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19724118 | lld:entrezgene |