1jrt
From Proteopedia
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|PDB= 1jrt |SIZE=350|CAPTION= <scene name='initialview01'>1jrt</scene>, resolution 1.7Å | |PDB= 1jrt |SIZE=350|CAPTION= <scene name='initialview01'>1jrt</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jrt OCA], [http://www.ebi.ac.uk/pdbsum/1jrt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jrt RCSB]</span> | ||
}} | }} | ||
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[[Category: Harrison, R W.]] | [[Category: Harrison, R W.]] | ||
[[Category: Kurinov, I V.]] | [[Category: Kurinov, I V.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CA]] | ||
[[Category: digestion]] | [[Category: digestion]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''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 21:38:02 2008'' |
Revision as of 18:38, 30 March 2008
| |||||||
| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HEMIACETAL COMPLEX BETWEEN LEUPEPTIN AND TRYPSIN
Overview
Three-dimensional structures of trypsin with the reversible inhibitor leupeptin have been determined in two different crystal forms. The first structure was determined at 1.7 A resolution with R-factor = 17.7% in the trigonal crystal space group P3(1)21, with unit cell dimensions of a = b = 55.62 A, c = 110.51 A. The second structure was determined at a resolution of 1.8 A with R-factor = 17.5% in the orthorhombic space group P2(1)2(1)2(1), with unit cell dimensions of a = 63.69 A, b = 69.37 A, c = 63.01 A. The overall protein structure is very similar in both crystal forms, with RMS difference for main-chain atoms of 0.27 A. The leupeptin backbone forms four hydrogen bonds with trypsin and a fifth hydrogen bond interaction is mediated by a water molecule. The aldehyde carbonyl of leupeptin forms a covalent bond of 1.42 A length with side-chain oxygen of Ser-195 in the active site. The reaction of trypsin with leupeptin proceeds through the formation of stable tetrahedral complex in which the hemiacetal oxygen atom is pointing out of the oxyanion hole and forming a hydrogen bond with His-57.
About this Structure
1JRT is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Two crystal structures of the leupeptin-trypsin complex., Kurinov IV, Harrison RW, Protein Sci. 1996 Apr;5(4):752-8. PMID:8845765
Page seeded by OCA on Sun Mar 30 21:38:02 2008
Categories: Bos taurus | Single protein | Trypsin | Harrison, R W. | Kurinov, I V. | Digestion | Hydrolase | Pancrea | Serine protease | Zymogen
