1lgy
From Proteopedia
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|SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lgy OCA], [http://www.ebi.ac.uk/pdbsum/1lgy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lgy RCSB]</span> | ||
}} | }} | ||
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[[Category: lipase]] | [[Category: lipase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:02:40 2008'' |
Revision as of 19:02, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
LIPASE II FROM RHIZOPUS NIVEUS
Overview
The crystal and molecular structure of Lipase II from Rhizopus niveus was analyzed using X-ray single crystal diffraction data at a resolution of 2.2 A. The structure was refined to an R-factor of 0.19 for all available data. This lipase was purified and crystallized as Lipase I, which contains two polypeptide chains combined through non-covalent interaction. However, during crystal growth, Lipase I was converted to Lipase II, which consists of a single polypeptide chain of 269 amino acid residues, by limited proteolysis. The structure of Lipase II shows a typical alpha/beta hydrolase fold containing the so-called nucleophilic elbow. The catalytic center of this enzyme is analogous to those of other neutral lipases and serine proteases. This catalytic center is sheltered by an alpha-helix lid, which appears in neutral lipases, opening the active site at the oil-water interface.
About this Structure
1LGY is a Single protein structure of sequence from Rhizopus niveus. Full crystallographic information is available from OCA.
Reference
The crystal structure of lipase II from Rhizopus niveus at 2.2 A resolution., Kohno M, Funatsu J, Mikami B, Kugimiya W, Matsuo T, Morita Y, J Biochem. 1996 Sep;120(3):505-10. PMID:8902613
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