1mee: Difference between revisions
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[[Image:1mee.gif|left|200px]] | [[Image:1mee.gif|left|200px]] | ||
'''THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C''' | {{Structure | ||
|PDB= 1mee |SIZE=350|CAPTION= <scene name='initialview01'>1mee</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] | |||
|GENE= | |||
}} | |||
'''THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MEE is a [ | 1MEE is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEE OCA]. | ||
==Reference== | ==Reference== | ||
Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C., Dauter Z, Betzel C, Genov N, Pipon N, Wilson KS, Acta Crystallogr B. 1991 Oct 1;47 ( Pt 5):707-30. PMID:[http:// | Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C., Dauter Z, Betzel C, Genov N, Pipon N, Wilson KS, Acta Crystallogr B. 1991 Oct 1;47 ( Pt 5):707-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1793542 1793542] | ||
[[Category: Bacillus pumilus]] | [[Category: Bacillus pumilus]] | ||
[[Category: Hirudo medicinalis]] | [[Category: Hirudo medicinalis]] | ||
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[[Category: complex(serine proteinase-inhibitor)]] | [[Category: complex(serine proteinase-inhibitor)]] | ||
''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 12:42:27 2008'' | ||
Revision as of 13:42, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C
OverviewOverview
The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.
About this StructureAbout this Structure
1MEE is a Protein complex structure of sequences from Bacillus pumilus and Hirudo medicinalis. Full crystallographic information is available from OCA.
ReferenceReference
Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C., Dauter Z, Betzel C, Genov N, Pipon N, Wilson KS, Acta Crystallogr B. 1991 Oct 1;47 ( Pt 5):707-30. PMID:1793542
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