1k9b: Difference between revisions

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-[[Image:1k9b.jpg|left|200px]]
- {{Structure
+==Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation==
-|PDB= 1k9b |SIZE=350|CAPTION= <scene name='initialview01'>1k9b</scene>, resolution 2.8&Aring;
+<StructureSection load='1k9b' size='340' side='right'caption='[[1k9b]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1k9b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K9B FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k9b OCA], [https://pdbe.org/1k9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k9b RCSB], [https://www.ebi.ac.uk/pdbsum/1k9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k9b ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=[[1d6r|1D6R]], [[1bbi|1BBI]], [[1pbi|1PBI]], [[1c2a|1C2A]], [[1pi2|1PI2]]
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k9b OCA], [http://www.ebi.ac.uk/pdbsum/1k9b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k9b RCSB]</span>
+[https://www.uniprot.org/uniprot/IBB1_SOYBN IBB1_SOYBN] Inhibitor of trypsin and of chymotrypsin.
-}}
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/1k9b_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k9b ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Bowman-Birk inhibitor from soybean is a small protein that contains a binary arrangement of trypsin-reactive and chymotrypsin-reactive subdomains. In this report, the crystal structure of this anticarcinogenic protein has been determined to 0.28-nm resolution by molecular replacement from crystals grown at neutral pH. The crystal structure differs from a previously determined NMR structure [Werner, M. H. &amp; Wemmer, D. E. (1992) Biochemistry 31, 999-1010] in the relative orientation of the two enzyme-insertion loops, in some details of the main chain trace, in the presence of favourable contacts in the trypsin-insertion loop, and in the orientation of several amino acid side chains. The proximity of Met27 and Gln48 in the X-ray structure contradicts the solution structure, in which these two side chains point away from each other. The significant effect of a Met27--&gt;Ile replacement on the inhibitory activity of the chymotrypsin-reactive subdomain agrees with the X-ray structure. Exposed hydrophobic patches, the presence of charged amino acid residues, and the presence of water molecules in the protein interior are in contrast to standard proteins that comprise a hydrophobic core and exposed polar amino acids.
-'''Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation'''
+Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation.,Voss RH, Ermler U, Essen LO, Wenzl G, Kim YM, Flecker P Eur J Biochem. 1996 Nov 15;242(1):122-31. PMID:8954162<ref>PMID:8954162</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1k9b" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The Bowman-Birk inhibitor from soybean is a small protein that contains a binary arrangement of trypsin-reactive and chymotrypsin-reactive subdomains. In this report, the crystal structure of this anticarcinogenic protein has been determined to 0.28-nm resolution by molecular replacement from crystals grown at neutral pH. The crystal structure differs from a previously determined NMR structure [Werner, M. H. &amp; Wemmer, D. E. (1992) Biochemistry 31, 999-1010] in the relative orientation of the two enzyme-insertion loops, in some details of the main chain trace, in the presence of favourable contacts in the trypsin-insertion loop, and in the orientation of several amino acid side chains. The proximity of Met27 and Gln48 in the X-ray structure contradicts the solution structure, in which these two side chains point away from each other. The significant effect of a Met27--&gt;Ile replacement on the inhibitory activity of the chymotrypsin-reactive subdomain agrees with the X-ray structure. Exposed hydrophobic patches, the presence of charged amino acid residues, and the presence of water molecules in the protein interior are in contrast to standard proteins that comprise a hydrophobic core and exposed polar amino acids.
+*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-K9B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9B OCA].
+__TOC__
+</StructureSection>
-==Reference==
-Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation., Voss RH, Ermler U, Essen LO, Wenzl G, Kim YM, Flecker P, Eur J Biochem. 1996 Nov 15;242(1):122-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8954162 8954162]
 [[Category: Glycine max]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Ermler, U.]]
+[[Category: Ermler U]]
-[[Category: Essen, L O.]]
+[[Category: Essen LO]]
-[[Category: Flecker, P.]]
+[[Category: Flecker P]]
-[[Category: Kim, Y M.]]
+[[Category: Kim YM]]
-[[Category: Voss, R H.]]
+[[Category: Voss RH]]
-[[Category: Wenzl, G.]]
+[[Category: Wenzl G]]
-[[Category: double-headed]]
-[[Category: tripple-stranded beta hairpin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:45:12 2008''