1gci

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[[Image:1gci.gif|left|200px]]<br /><applet load="1gci" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gci.gif|left|200px]]
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caption="1gci, resolution 0.78&Aring;" />
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'''THE 0.78 ANGSTROMS STRUCTURE OF A SERINE PROTEASE-BACILLUS LENTUS SUBTILISIN'''<br />
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{{Structure
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|PDB= 1gci |SIZE=350|CAPTION= <scene name='initialview01'>1gci</scene>, resolution 0.78&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE=
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}}
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'''THE 0.78 ANGSTROMS STRUCTURE OF A SERINE PROTEASE-BACILLUS LENTUS SUBTILISIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GCI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCI OCA].
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1GCI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GCI OCA].
==Reference==
==Reference==
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The 0.78 A structure of a serine protease: Bacillus lentus subtilisin., Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R, Biochemistry. 1998 Sep 29;37(39):13446-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9753430 9753430]
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The 0.78 A structure of a serine protease: Bacillus lentus subtilisin., Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R, Biochemistry. 1998 Sep 29;37(39):13446-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9753430 9753430]
[[Category: Bacillus lentus]]
[[Category: Bacillus lentus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: ultra-high resolution]]
[[Category: ultra-high resolution]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:21:19 2008''

Revision as of 09:21, 20 March 2008

Image:1gci.gif


PDB ID 1gci

Drag the structure with the mouse to rotate
, resolution 0.78Å
Ligands: , and
Activity: Subtilisin, with EC number 3.4.21.62
Coordinates: save as pdb, mmCIF, xml



THE 0.78 ANGSTROMS STRUCTURE OF A SERINE PROTEASE-BACILLUS LENTUS SUBTILISIN


Overview

Ultrahigh-resolution X-ray diffraction data from cryo-cooled, B. lentus subtilisin crystals has been collected to a resolution of 0.78 A. The refined model coordinates have a rms deviation of 0.22 A relative to the same structure determined at room temperature and 2.0 A resolution. Several regions of main-chain and side-chain disorder have been identified for 21 out of 269 residues in one polypeptide chain. Hydrogen atoms appear as significant peaks in the Fo - Fc difference electron density map, and carbon, nitrogen, and oxygen atoms can be differentiated. The estimated standard deviation (ESD) for all main-chain non-hydrogen bond lengths is 0.009 A and 0.5 degrees for bond angles based on an unrestrained full-matrix least-squares refinement. Hydrogen bonds are resolved in the serine protease catalytic triad (Ser-His-Asp). Electron density is observed for an unusual, short hydrogen bond between aspartic acid and histidine in the catalytic triad. The hydrogen atom, identified by NMR in numerous serine proteases, appears to be shared by the heteroatoms in the bond. This represents the first reported correlation between detailed chemical features identified by NMR and those in a cryo-cooled crystallographic structure determination at ultrahigh resolution. The short hydrogen bond, designated "catalytic hydrogen bond", occurs as part of an elaborate hydrogen bond network, involving Asp of the catalytic triad. While unusual, these features appear to have conserved analogues in other serine protease families although specific details differ from family to family.

About this Structure

1GCI is a Single protein structure of sequence from Bacillus lentus. Full crystallographic information is available from OCA.

Reference

The 0.78 A structure of a serine protease: Bacillus lentus subtilisin., Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R, Biochemistry. 1998 Sep 29;37(39):13446-52. PMID:9753430

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