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3b7r
From Proteopedia
(Difference between revisions)
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<StructureSection load='3b7r' size='340' side='right'caption='[[3b7r]], [[Resolution|resolution]] 1.81Å' scene=''> | <StructureSection load='3b7r' size='340' side='right'caption='[[3b7r]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3b7r]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3b7r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B7R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BIR:N-[3-[(1-AMINOETHYL)(HYDROXY)PHOSPHORYL]-2-(1,1-BIPHENYL-4-YLMETHYL)PROPANOYL]ALANINE'>BIR</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BIR:N-[3-[(1-AMINOETHYL)(HYDROXY)PHOSPHORYL]-2-(1,1-BIPHENYL-4-YLMETHYL)PROPANOYL]ALANINE'>BIR</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r59|2r59]], [[3b7s|3b7s]], [[3b7t|3b7t]], [[3b7u|3b7u]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2r59|2r59]], [[3b7s|3b7s]], [[3b7t|3b7t]], [[3b7u|3b7u]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LTA4H, LTA4 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LTA4H, LTA4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Leukotriene-A(4)_hydrolase Leukotriene-A(4) hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.6 3.3.2.6] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b7r OCA], [https://pdbe.org/3b7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b7r RCSB], [https://www.ebi.ac.uk/pdbsum/3b7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b7r ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/LKHA4_HUMAN LKHA4_HUMAN]] Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.<ref>PMID:1897988</ref> <ref>PMID:1975494</ref> <ref>PMID:2244921</ref> <ref>PMID:12207002</ref> <ref>PMID:11917124</ref> <ref>PMID:15078870</ref> <ref>PMID:18804029</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 11:27, 5 January 2022
Leukotriene A4 Hydrolase Complexed with Inhibitor RB3040
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Categories: Human | Large Structures | Fournie-Zaluski, M C | Haeggstrom, J | Muroya, A | Roques, B P | Tholander, F | Thunnissen, M | Alternative splicing | Analogue peptide | Cytoplasm | Hydrolase | Hydrolysis | Leukotriene biosynthesis | Metal-binding | Metalloprotease | Multifunctional enzyme | Protease | Transition state | Zinc

