1f6w: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1f6w.jpg|left|200px]] | [[Image:1f6w.jpg|left|200px]] | ||
'''STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE''' | {{Structure | ||
|PDB= 1f6w |SIZE=350|CAPTION= <scene name='initialview01'>1f6w</scene>, resolution 2.30Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE''' | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
1F6W is a [ | 1F6W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of the catalytic domain of human bile salt activated lipase., Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC, Protein Sci. 2000 Sep;9(9):1783-90. PMID:[http:// | Crystal structure of the catalytic domain of human bile salt activated lipase., Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC, Protein Sci. 2000 Sep;9(9):1783-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11045623 11045623] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 23: | Line 32: | ||
[[Category: esterase]] | [[Category: esterase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:05:13 2008'' | ||
Revision as of 12:05, 20 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Triacylglycerol lipase, with EC number 3.1.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE
OverviewOverview
Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a variety of lipids in the small intestine. A distinct property of BAL is its dependency on bile salts in hydrolyzing substrates of long acyl chains or bulky alcoholic motifs. A crystal structure of the catalytic domain of human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has been determined at 2.3 A resolution. The crystal form belongs to space group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein shows an alpha/beta hydrolase fold. In the absence of bound bile salt molecules, the protein possesses a preformed catalytic triad and a functional oxyanion hole. Several surface loops around the active site are mobile, including two loops potentially involved in substrate binding (residues 115-125 and 270-285).
DiseaseDisease
Known disease associated with this structure: Maturity-onset diabetes of the young, type VIII OMIM:[114840]
About this StructureAbout this Structure
1F6W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the catalytic domain of human bile salt activated lipase., Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC, Protein Sci. 2000 Sep;9(9):1783-90. PMID:11045623
Page seeded by OCA on Thu Mar 20 11:05:13 2008