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PDBe Entry: 1zj5 view

Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, C123S, A134S, S208G, A229V, K234R) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.7 A
Summary
Header Hydrolasesearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.7 Å, R-factor: 18.4%, Free R-factor: 21.0%, Spacegroup: P 21 21 21
Released 05/07/2005, deposition: 28/04/2005, last revision: 24/02/2009
Authors Kim, H.-K.search; Liu, J.-W.search; Carr, P.D.search; Ollis, D.L.search
Primary citation Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
ACTA CRYSTALLOGR.,SECT.Dsearch vol:61, pag:920-931 (2005) [PubMed ID 15983415 ]search
Keywords alpha and beta proteinssearch, 3-D structuresearch, Serine esterasesearch, Hydrolasesearch, Aromatic hydrocarbons catabolismsearch, PMSFsearch
EC 3.1.1.45 ExPASy BRENDA search (A)
Organism Pseudomonas putida 303search(A)
UniProt Carboxymethylenebutenolidase (EC 3.1.1.45) (Dienelactone hydrolase) (DLH) P0A114search (A)
Solvent A
Related entries 1din, 1ggv, 1zi6, 1zi8, 1zi9, 1zic, 1zix, 1ziy, 1zj4
Polymers
Id Name Type UniProt Residues Observed
A Carboxymethylenebutenolidase Protein P0A114 (CLCD_PSEPU)search
236 98%
Heterogens
Id Name Ligands
A SULFATE ION SO4 search
A GLYCEROL GOL search
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