4wbc: Difference between revisions
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<StructureSection load='4wbc' size='340' side='right'caption='[[4wbc]], [[Resolution|resolution]] 2.14Å' scene=''> | <StructureSection load='4wbc' size='340' side='right'caption='[[4wbc]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wbc]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4wbc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Psophocarpus_tetragonolobus Psophocarpus tetragonolobus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3wbc 3wbc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WBC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.138Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wbc OCA], [https://pdbe.org/4wbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wbc RCSB], [https://www.ebi.ac.uk/pdbsum/4wbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wbc ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ICW3_PSOTE ICW3_PSOTE] Inhibits alpha-chymotrypsin at the molar ratio of 1:2 in state of 1:1. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Psophocarpus tetragonolobus]] | [[Category: Psophocarpus tetragonolobus]] | ||
[[Category: Chakrabarti | [[Category: Chakrabarti C]] | ||
[[Category: Dattagupta | [[Category: Dattagupta JK]] | ||
[[Category: Ravichandran | [[Category: Ravichandran S]] | ||
[[Category: Sen | [[Category: Sen U]] | ||
Latest revision as of 03:52, 28 December 2023
2.13 A STRUCTURE OF A KUNITZ-TYPE WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN2.13 A STRUCTURE OF A KUNITZ-TYPE WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN
Structural highlights
FunctionICW3_PSOTE Inhibits alpha-chymotrypsin at the molar ratio of 1:2 in state of 1:1. 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 crystal structure of a Kunitz-type double-headed alpha--chymotrypsin inhibitor from winged bean seeds has been refined at 2.13 A resolution using data collected from cryo-cooled (90 K) crystals which belong to the hexagonal space group P6(1)22 with unit-cell parameters a = b = 60.84, c = 207.91 A. The volume of the unit cell is reduced by 5.3% on cooling. The refinement converged to an R value of 20.0% (R(free) = 25.8%) for 11100 unique reflections and the model shows good stereochemistry, with r.m.s. deviations from ideal values for bond lengths and bond angles of 0.011 A and 1.4 degrees, respectively. The structural architecture of the protein consists of 12 antiparallel beta-strands joined in the form of a characteristic beta-trefoil fold, with the two reactive-site regions, Asn38-Leu43 and Gln63-Phe68, situated on two external loops. Although the overall protein fold is the same as that of the room-temperature model, some conformational changes are observed in the loop regions and in the side chains of a few surface residues. A total of 176 ordered water molecules and five sulfate ions are included in the model. Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K structure of winged bean chymotrypsin inhibitor (WCI) at 2.13 A resolution.,Ravichandran S, Sen U, Chakrabarti C, Dattagupta JK Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1814-21. PMID:10531477[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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