1hsr
From Proteopedia
(Difference between revisions)
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<StructureSection load='1hsr' size='340' side='right'caption='[[1hsr]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1hsr' size='340' side='right'caption='[[1hsr]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1hsr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/' | + | <table><tr><td colspan='2'>[[1hsr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agaricales_sp._'Arthromyces_ramosus' Agaricales sp. 'Arthromyces ramosus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HSR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BHO:BENZHYDROXAMIC+ACID'>BHO</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BHO:BENZHYDROXAMIC+ACID'>BHO</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1hsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsr OCA], [https://pdbe.org/1hsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hsr RCSB], [https://www.ebi.ac.uk/pdbsum/1hsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hsr ProSAT]</span></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=1hsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsr OCA], [https://pdbe.org/1hsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hsr RCSB], [https://www.ebi.ac.uk/pdbsum/1hsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hsr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PER_ARTRA PER_ARTRA] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1hsr ConSurf]. | </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=1hsr ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of Arthromyces ramosus peroxidase (ARP) in complex with benzhydroxamic acid (BHA) as determined by X-ray analysis at 1.6 A shows unambiguously how BHA binds to ARP. BHA is located in the distal heme pocket. Its functional groups are held by three hydrogen bonds to His56N(epsilon), Arg52N(epsilon), and Pro(154)O, but are too far away to interact with the heme iron. The aromatic ring of BHA is positioned at the entrance of the channel to the heme pocket, approximately parallel to the heme group. Most water molecules at the active site of the native enzyme are replaced by BHA, leaving a ligand, probably a water molecule, at the sixth position of the heme. Results are compared with spectroscopic data. | ||
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| - | Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X-ray crystallographic analysis of the complex at 1.6 A resolution.,Itakura H, Oda Y, Fukuyama K FEBS Lett. 1997 Jul 21;412(1):107-10. PMID:9257700<ref>PMID:9257700</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1hsr" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Arthromyces ramosus]] | + | [[Category: Agaricales sp. 'Arthromyces ramosus']] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Fukuyama K]] | |
| - | [[Category: Fukuyama | + | [[Category: Itakura H]] |
| - | [[Category: Itakura | + | |
| - | + | ||
| - | + | ||
Revision as of 11:35, 27 March 2024
BINDING MODE OF BENZHYDROXAMIC ACID TO ARTHROMYCES RAMOSUS PEROXIDASE
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