1ept
From Proteopedia
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- | [[Image:1ept.gif|left|200px]] | + | [[Image:1ept.gif|left|200px]] |
- | + | ||
- | '''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN''' | + | {{Structure |
+ | |PDB= 1ept |SIZE=350|CAPTION= <scene name='initialview01'>1ept</scene>, resolution 1.8Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</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= | ||
+ | }} | ||
+ | |||
+ | '''REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1EPT is a [ | + | 1EPT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EPT OCA]. |
==Reference== | ==Reference== | ||
- | Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin., Huang Q, Wang Z, Li Y, Liu S, Tang Y, Biochim Biophys Acta. 1994 Nov 16;1209(1):77-82. PMID:[http:// | + | Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin., Huang Q, Wang Z, Li Y, Liu S, Tang Y, Biochim Biophys Acta. 1994 Nov 16;1209(1):77-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7947985 7947985] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: hydrolase (serine protease)]] | [[Category: hydrolase (serine protease)]] | ||
- | ''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 10:58:48 2008'' |
Revision as of 08:58, 20 March 2008
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, resolution 1.8Å | |||||||
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Ligands: | |||||||
Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
REFINED 1.8 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF PORCINE EPSILON-TRYPSIN
Overview
Porcine epsilon-trypsin is a three-chain inactivated trypsin from the limited autolysis of porcine beta-trypsin. It is cleaved at positions Lys60-Ser61 and Lys145-Ser146. The crystal structure has been determined by using the molecular replacement method, and refined at 1.8 A resolution. The R-value of final model is 0.184. Comparison with the electron density map of porcine beta-trypsin (PTRY) in complex (BBIT), and with that of native bovine beta-trypsin (HTNA), revealed no obvious changes except at the autolysis positions, and no changes at the active center were observed. The autolysis at positions Lys60-Ser61 and Lys145-Ser146 does not affect the conformation of His-57 in the active center and therefore cannot explain for a loss in porcine epsilon-trypsin activity.
About this Structure
1EPT is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Refined 1.8 A resolution crystal structure of the porcine epsilon-trypsin., Huang Q, Wang Z, Li Y, Liu S, Tang Y, Biochim Biophys Acta. 1994 Nov 16;1209(1):77-82. PMID:7947985
Page seeded by OCA on Thu Mar 20 10:58:48 2008
Categories: Protein complex | Sus scrofa | Trypsin | Huang, Q. | Li, Y. | Liu, S. | Tang, Y. | Wang, Z. | CA | Hydrolase (serine protease)