1aks: Difference between revisions
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[[Image:1aks.jpg|left|200px]] | [[Image:1aks.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN''' | {{Structure | ||
|PDB= 1aks |SIZE=350|CAPTION= <scene name='initialview01'>1aks</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= | |||
}} | |||
'''CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AKS is a [ | 1AKS 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=1AKS OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15299934 15299934] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: serine protease]] | [[Category: 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 09:58:56 2008'' | ||
Revision as of 07:59, 20 March 2008
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| 1aks, resolution 1.8Å | |||||||||||||
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| Ligands: | CA | ||||||||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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