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1acb

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[[Image:1acb.gif|left|200px]]
 
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{{Structure
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==CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION==
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|PDB= 1acb |SIZE=350|CAPTION= <scene name='initialview01'>1acb</scene>, resolution 2.0&Aring;
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<StructureSection load='1acb' size='340' side='right'caption='[[1acb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1acb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ACB FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1]
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</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&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1acb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1acb OCA], [https://pdbe.org/1acb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1acb RCSB], [https://www.ebi.ac.uk/pdbsum/1acb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1acb ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ac/1acb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1acb ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION'''
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==See Also==
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*[[Chymotrypsin 3D structures|Chymotrypsin 3D structures]]
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*[[Eglin|Eglin]]
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==Overview==
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__TOC__
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The crystal structure of the complex between bovine alpha-chymotrypsin and the leech (Hirudo medicinalis) protein proteinase inhibitor eglin c has been refined at 2.0 A resolution to a crystallographic R-factor of 0.167. The structure of the complex includes 2290 protein and 143 solvent atoms. Eglin c is bound to the cognate enzyme through interactions involving 11 residues of the inhibitor (sites P5-P4' in the reactive site loop, P10' and P23') and 17 residues from chymotrypsin. Binding of eglin c to the enzyme causes a contained hinge-bending movement around residues P4 and P4' of the inhibitor. The tertiary structure of chymotrypsin is little affected, with the exception of the 10-13 region, where an ordered structure for the polypeptide chain is observed. The overall binding mode is consistent with those found in other serine proteinase-protein-inhibitor complexes, including those from different inhibition families. Contained, but significant differences are observed in the establishment of intramolecular hydrogen bonds and polar interactions stabilizing the structure of the intact inhibitor, if the structure of eglin c in its complex with chymotrypsin is compared with that of other eglin c-serine proteinase complexes.
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</StructureSection>
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[[Category: Bos taurus]]
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==About this Structure==
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[[Category: Hirudo medicinalis]]
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1ACB is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACB OCA].
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[[Category: Large Structures]]
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[[Category: Amiconi G]]
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==Reference==
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[[Category: Ascenzi P]]
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Crystal and molecular structure of the bovine alpha-chymotrypsin-eglin c complex at 2.0 A resolution., Frigerio F, Coda A, Pugliese L, Lionetti C, Menegatti E, Amiconi G, Schnebli HP, Ascenzi P, Bolognesi M, J Mol Biol. 1992 May 5;225(1):107-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1583684 1583684]
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[[Category: Bolognesi M]]
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[[Category: Chymotrypsin]]
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[[Category: Coda A]]
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[[Category: Protein complex]]
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[[Category: Frigerio F]]
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[[Category: Amiconi, G.]]
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[[Category: Lionetti C]]
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[[Category: Ascenzi, P.]]
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[[Category: Menegatti E]]
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[[Category: Bolognesi, M.]]
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[[Category: Pugliese L]]
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[[Category: Coda, A.]]
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[[Category: Schnebli HP]]
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[[Category: Frigerio, F.]]
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[[Category: Lionetti, C.]]
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[[Category: Menegatti, E.]]
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[[Category: Pugliese, L.]]
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[[Category: Schnebli, H P.]]
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[[Category: hydrolase(serine protease)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:55:46 2008''
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Current revision

CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION

PDB ID 1acb

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