1tec
From Proteopedia
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|PDB= 1tec |SIZE=350|CAPTION= <scene name='initialview01'>1tec</scene>, resolution 2.2Å | |PDB= 1tec |SIZE=350|CAPTION= <scene name='initialview01'>1tec</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Thermitase Thermitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.66 3.4.21.66] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermitase Thermitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.66 3.4.21.66] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tec OCA], [http://www.ebi.ac.uk/pdbsum/1tec PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tec RCSB]</span> | ||
}} | }} | ||
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[[Category: Gros, P.]] | [[Category: Gros, P.]] | ||
[[Category: Hol, W G.J.]] | [[Category: Hol, W G.J.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: NA]] | ||
[[Category: complex(serine proteinase-inhibitor)]] | [[Category: complex(serine proteinase-inhibitor)]] | ||
| - | ''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 23:54:52 2008'' |
Revision as of 20:55, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Thermitase, with EC number 3.4.21.66 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTALLOGRAPHIC REFINEMENT BY INCORPORATION OF MOLECULAR DYNAMICS. THE THERMOSTABLE SERINE PROTEASE THERMITASE COMPLEXED WITH EGLIN-C
Overview
In order to investigate the principles of protein thermostability, the crystal structure of thermitase from Thermoactinomyces vulgaris, a thermostable member of the subtilisin family of serine proteases, has been determined in a complex with eglin c. Eglin c is a serine protease inhibitor from the leech Hirudo medicinalis. After data collection with a television area-detector diffractometer and initial structure solution by molecular-replacement methods, crystallographic refinement proceeded with incorporation of molecular-dynamics techniques. It appeared that this refinement procedure has a large convergence radius with movements of more than 5 A for many atoms. Two procedures for the crystallographic molecular-dynamics refinement have been tested. They differed mainly in time span and weight on the X-ray 'energy'. The best results were obtained with a procedure which allowed the molecular-dynamics technique to search a large area in conformational space by having less weight on the X-ray restraints and allowing more time. The use of molecular-dynamics refinement considerably simplified the laborious and difficult task of fitting the model in its electron density during the refinement process. The final crystallographic R factor is 17.9% at 2.2 A resolution.
About this Structure
1TEC is a Protein complex structure of sequences from Hirudo medicinalis and Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.
Reference
Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c., Gros P, Fujinaga M, Dijkstra BW, Kalk KH, Hol WG, Acta Crystallogr B. 1989 Oct 1;45 ( Pt 5):488-99. PMID:2688688
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