1TAH
THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE
Summary for 1TAH
Entry DOI | 10.2210/pdb1tah/pdb |
Descriptor | LIPASE, CALCIUM ION (2 entities in total) |
Functional Keywords | hydrolase(carboxylic esterase) |
Biological source | Burkholderia glumae |
Cellular location | Secreted : Q05489 |
Total number of polymer chains | 4 |
Total formula weight | 132346.81 |
Authors | Noble, M.E.M.,Cleasby, A.,Johnson, L.N.,Egmond, M.,Frenken, L.G.J. (deposition date: 1993-12-21, release date: 1994-05-31, Last modification date: 2017-11-29) |
Primary citation | Noble, M.E.,Cleasby, A.,Johnson, L.N.,Egmond, M.R.,Frenken, L.G. The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett., 331:123-128, 1993 Cited by PubMed: 8405390DOI: 10.1016/0014-5793(93)80310-Q PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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