1wav: Difference between revisions
No edit summary |
No edit summary |
||
(2 intermediate revisions by the same user not shown) | |||
Line 3: | Line 3: | ||
<StructureSection load='1wav' size='340' side='right'caption='[[1wav]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1wav' size='340' side='right'caption='[[1wav]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1wav]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1wav]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAV FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPH:PHENOL'>IPH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.5Å</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=IPH:PHENOL'>IPH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1wav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wav OCA], [https://pdbe.org/1wav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wav RCSB], [https://www.ebi.ac.uk/pdbsum/1wav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wav ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/INS_PIG INS_PIG] Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 14: | Line 15: | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wa/1wav_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wa/1wav_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
Line 37: | Line 38: | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Chang | [[Category: Chang W-R]] | ||
[[Category: Ding | [[Category: Ding J-H]] | ||
[[Category: Liang | [[Category: Liang D-C]] | ||
[[Category: Wan | [[Category: Wan Z-L]] | ||
Latest revision as of 10:34, 30 October 2024
CRYSTAL STRUCTURE OF FORM B MONOCLINIC CRYSTAL OF INSULINCRYSTAL STRUCTURE OF FORM B MONOCLINIC CRYSTAL OF INSULIN
Structural highlights
FunctionINS_PIG Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. 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 form-B monoclinic insulin crystal was obtained from the sodium citrate buffer with 1% zinc chloride, keeping phenolic content between 0.76% and 1.25%. Its space group is P2(1), cell constants are: a = 4.924 nm, b = 6.094 nm, c = 4.818 nm, beta = 95.8 degrees. There are 6 insulin molecules which form a hexamer. The initial phase was obtained by using rotation function program of X-PLOR program package and molecular packing program of our laboratory. The molecular model was chosen from 4 zinc bovine insulin hexamer. After the preliminary refinement by using the macromolecular rigid body refinement technique, the molecular model was further refined and adjusted by using the energy-minimizing stereochemically restrained least-squared refinement on the difference Fourier maps. The final R-factor is 22.4% at 0.3 nm resolution, the r.m.s. deviations from standard bond length and bond angle are 0.0022 nm and 4.7 degrees, respectively. Molecular replacement study on form-B monoclinic crystal of insulin.,Ding J, Wan Z, Chang W, Liang D Sci China C Life Sci. 1996 Apr;39(2):144-53. PMID:8760462[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
|