1a7s: Difference between revisions

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-[[Image:1a7s.png|left|200px]]
-<!--
+==ATOMIC RESOLUTION STRUCTURE OF HBP==
-The line below this paragraph, containing "STRUCTURE_1a7s", creates the "Structure Box" on the page.
+<StructureSection load='1a7s' size='340' side='right'caption='[[1a7s]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1a7s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7S FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.12&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-{{STRUCTURE_1a7s|  PDB=1a7s  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a7s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7s OCA], [https://pdbe.org/1a7s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7s RCSB], [https://www.ebi.ac.uk/pdbsum/1a7s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7s ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CAP7_HUMAN CAP7_HUMAN] This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G.<ref>PMID:1937776</ref> <ref>PMID:1399008</ref>
+== 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/a7/1a7s_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=1a7s ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Crystals of human heparin binding protein (HBP) diffract to 1.1 A when flash-frozen at 120 K. The atomic resolution structure has been refined anisotropically using SHELXL96. The final model of HBP consists of 221 amino-acid residues of 225 possible, three glycosylation units, one chloride ion, 15 precipitant ethanol molecules and 323 water molecules. The structure is refined to a final crystallographic R factor of 15.9% and Rfree(5%) of 18.9% using all data. A putative protein kinase C activation site has been identified, involving residues 113-120. The structure is compared to the previously determined 2.3 A resolution structure of HBP.
-===ATOMIC RESOLUTION STRUCTURE OF HBP===
+Atomic resolution structure of human HBP/CAP37/azurocidin.,Karlsen S, Iversen LF, Larsen IK, Flodgaard HJ, Kastrup JS Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):598-609. PMID:9761855<ref>PMID:9761855</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_9761855}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1a7s" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 9761855 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9761855}}
+__TOC__
+</StructureSection>
-==About this Structure==
-[[1a7s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7S OCA].
-==Reference==
-<ref group="xtra">PMID:009761855</ref><ref group="xtra">PMID:011917145</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Flodgaard, H J.]]
+[[Category: Large Structures]]
-[[Category: Iversen, L F.]]
+[[Category: Flodgaard HJ]]
-[[Category: Karlsen, S.]]
+[[Category: Iversen LF]]
-[[Category: Kastrup, J S.]]
+[[Category: Karlsen S]]
-[[Category: Larsen, I K.]]
+[[Category: Kastrup JS]]
-[[Category: Endotoxin binding]]
+[[Category: Larsen IK]]
-[[Category: Heparin]]
-[[Category: Serine protease homolog]]