1smd: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1smd.gif|left|200px]] | [[Image:1smd.gif|left|200px]] | ||
'''HUMAN SALIVARY AMYLASE''' | {{Structure | ||
|PDB= 1smd |SIZE=350|CAPTION= <scene name='initialview01'>1smd</scene>, resolution 1.6Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] | |||
|GENE= | |||
}} | |||
'''HUMAN SALIVARY AMYLASE''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1SMD is a [ | 1SMD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1SMD with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb74_1.html Alpha-amylase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SMD OCA]. | ||
==Reference== | ==Reference== | ||
Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity., Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):435-46. PMID:[http:// | Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity., Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):435-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299664 15299664] | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| Line 21: | Line 30: | ||
[[Category: o-glycosyl]] | [[Category: o-glycosyl]] | ||
''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 14:06:51 2008'' | ||
Revision as of 15:06, 20 March 2008
| |||||||
| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN SALIVARY AMYLASE
OverviewOverview
Salivary alpha-amylase, a major component of human saliva, plays a role in the initial digestion of starch and may be involved in the colonization of bacteria involved in early dental plaque formation. The three-dimensional atomic structure of salivary amylase has been determined to understand the structure-function relationships of this enzyme. This structure was refined to an R value of 18.4% with 496 amino-acid residues, one calcium ion, one chloride ion and 170 water molecules. Salivary amylase folds into a multidomain structure consisting of three domains, A, B and C. Domain A has a (beta/alpha)(8-) barrel structure, domain B has no definite topology and domain C has a Greek-key barrel structure. The Ca(2+) ion is bound to Asnl00, Arg158, Asp167, His201 and three water molecules. The Cl(-) ion is bound to Arg195, Asn298 and Arg337 and one water molecule. The highly mobile glycine-rich loop 304-310 may act as a gateway for substrate binding and be involved in a 'trap-release' mechanism in the hydrolysis of substrates. Strategic placement of calcium and chloride ions, as well as histidine and tryptophan residues may play a role in differentiating between the glycone and aglycone ends of the polysaccharide substrates. Salivary amylase also possesses a suitable site for binding to enamel surfaces and provides potential sites for the binding of bacterial adhesins.
About this StructureAbout this Structure
1SMD is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1SMD with [Alpha-amylase]. Full crystallographic information is available from OCA.
ReferenceReference
Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity., Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):435-46. PMID:15299664
Page seeded by OCA on Thu Mar 20 14:06:51 2008