1bbi: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='1bbi' size='340' side='right'caption='[[1bbi]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='1bbi' size='340' side='right'caption='[[1bbi]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1bbi]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1bbi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BBI FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bbi|2bbi]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2bbi|2bbi]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bbi OCA], [https://pdbe.org/1bbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bbi RCSB], [https://www.ebi.ac.uk/pdbsum/1bbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bbi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/IBB1_SOYBN IBB1_SOYBN]] Inhibitor of trypsin and of chymotrypsin. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Trypsin inhibitor|Trypsin inhibitor]] | *[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:27, 14 July 2021
THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTIONTHREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTION
Structural highlights
Function[IBB1_SOYBN] Inhibitor of trypsin and of chymotrypsin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution has been determined by two-dimensional 1H nuclear magnetic resonance spectroscopy and dynamical simulated annealing using the program XPLOR. The structure was defined by 907 NOEs involving intra- and interresidue contacts which served as distance constraints for a protocol of dynamical simulated annealing. In addition, 48 phi angle constraints involving non-proline amino acids, 29 chi angle constraints, six omega angle constraints for the X-Pro peptide bond, and 35 stereoassignments for prochiral centers were incorporated during the course of the calculation. The protein is characterized by two distinct binding domains for serine protease. Each domain is comprised of a beta-hairpin (antiparallel beta-sheet and a cis-proline-containing type VIb reverse turn) with a short segment making a third strand of antiparallel beta-sheet. The structure determination and refinement are described, and the structure is compared to other structures of Bowman-Birk inhibitors as well as other families of serine protease inhibitors. Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution.,Werner MH, Wemmer DE Biochemistry. 1992 Feb 4;31(4):999-1010. PMID:1734975[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||