5MAL
Crystal structure of extracelular lipase from Streptomyces rimosus at 1.7A resolution
Summary for 5MAL
Entry DOI | 10.2210/pdb5mal/pdb |
Descriptor | Lipase (2 entities in total) |
Functional Keywords | sgnh hydrolase, multifunctional enzyme from streptomyces rimosus, quantum-mechanical study, catalytic mechanism, catalytic dyad - ser /his, hydrolase |
Biological source | Streptomyces rimosus |
Cellular location | Secreted {ECO:0000269|Ref: Q93MW7 |
Total number of polymer chains | 2 |
Total formula weight | 48387.48 |
Authors | Stefanic, Z. (deposition date: 2016-11-03, release date: 2017-06-14, Last modification date: 2024-01-17) |
Primary citation | Lescic Asler, I.,Stefanic, Z.,Marsavelski, A.,Vianello, R.,Kojic-Prodic, B. Catalytic Dyad in the SGNH Hydrolase Superfamily: In-depth Insight into Structural Parameters Tuning the Catalytic Process of Extracellular Lipase from Streptomyces rimosus. ACS Chem. Biol., 12:1928-1936, 2017 Cited by PubMed: 28558229DOI: 10.1021/acschembio.6b01140 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.708 Å) |
Structure validation
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