1tx7: Difference between revisions
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[[Image:1tx7.gif|left|200px]] | [[Image:1tx7.gif|left|200px]] | ||
'''Bovine Trypsin complexed with p-amidinophenylmethylphosphinic acid (AMPA)''' | {{Structure | ||
|PDB= 1tx7 |SIZE=350|CAPTION= <scene name='initialview01'>1tx7</scene>, resolution 1.75Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=4CM:(4-CARBAMIMIDOYLPHENYL)-METHYL-PHOSPHINIC ACID'>4CM</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | |||
|GENE= | |||
}} | |||
'''Bovine Trypsin complexed with p-amidinophenylmethylphosphinic acid (AMPA)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1TX7 is a [ | 1TX7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TX7 OCA]. | ||
==Reference== | ==Reference== | ||
An oxyanion-hole selective serine protease inhibitor in complex with trypsin., Cui J, Marankan F, Fu W, Crich D, Mesecar A, Johnson ME, Bioorg Med Chem. 2002 Jan;10(1):41-6. PMID:[http:// | An oxyanion-hole selective serine protease inhibitor in complex with trypsin., Cui J, Marankan F, Fu W, Crich D, Mesecar A, Johnson ME, Bioorg Med Chem. 2002 Jan;10(1):41-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11738605 11738605] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trypsin]] | [[Category: trypsin]] | ||
''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 14:24:23 2008'' |
Revision as of 15:24, 20 March 2008
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, resolution 1.75Å | |||||||
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Ligands: | and | ||||||
Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Bovine Trypsin complexed with p-amidinophenylmethylphosphinic acid (AMPA)
OverviewOverview
p-amidinophenylmethylphosphinic acid (AMPA) was designed, synthesized and crystallized in complex with trypsin to study interactions with the oxyanion hole at the S1 site. In comparison to benzamidine, AMPA shows improved activity, which the crystal structure demonstrates to result from hydrogen bonds between the negatively charged phosphinic acid group and the catalytic residues at the oxyanion hole.
About this StructureAbout this Structure
1TX7 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
An oxyanion-hole selective serine protease inhibitor in complex with trypsin., Cui J, Marankan F, Fu W, Crich D, Mesecar A, Johnson ME, Bioorg Med Chem. 2002 Jan;10(1):41-6. PMID:11738605
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