1aks

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[[Image:1aks.jpg|left|200px]]
[[Image:1aks.jpg|left|200px]]
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{{Structure
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|PDB= 1aks |SIZE=350|CAPTION= <scene name='initialview01'>1aks</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1aks", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1aks| PDB=1aks | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aks OCA], [http://www.ebi.ac.uk/pdbsum/1aks PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aks RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN'''
'''CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN'''
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[[Category: Pattabhi, V.]]
[[Category: Pattabhi, V.]]
[[Category: Sundaram, P V.]]
[[Category: Sundaram, P V.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: serine protease]]
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[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:23:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:42:20 2008''
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Revision as of 07:23, 2 May 2008

Template:STRUCTURE 1aks

CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN


Overview

The first crystal structure of an active autolysate form of porcine alpha-trypsin (APT), a two-chain molecule obtained from the limited autolysis of porcine beta-trypsin at position Lys145-Ser146, has been determined. APT crystallizes in space group P2(1)2(1)2(1) with one protein molecule in the asymmetric unit. The structure was solved by molecular replacement followed by refinement using X-PLOR to an R factor of 0.200 and an R(free) of 0.285 for 8.0-1.8 A data with r.m.s deviations from ideal values of 0.01 A and 1.7 degrees for bond lengths and bond angles, respectively. Comparison with inactive autolysate porcine epsilon-trypsin (EPT) and porcine beta-trypsin in complex with bittergourd trypsin inhibitor (MCT) revealed a small but systematic directional chain shift around the active-site residues from APT to EPT to MCT.

About this Structure

1AKS is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

Reference

The first structure at 1.8 A resolution of an active autolysate form of porcine alpha-trysoin., Johnson A, Krishnaswamy S, Sundaram PV, Pattabhi V, Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):311-5. PMID:15299934 Page seeded by OCA on Fri May 2 10:23:56 2008

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