8ho5
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Falcilysin in complex with MMV665806== | |
| - | + | <StructureSection load='8ho5' size='340' side='right'caption='[[8ho5]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8ho5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HO5 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.003Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=XUN:(2S)-1-(2,3-dimethyl-1H-indol-1-yl)-3-{[(1S,2S)-2-methylcyclohexyl]amino}propan-2-ol'>XUN</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=8ho5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ho5 OCA], [https://pdbe.org/8ho5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ho5 RCSB], [https://www.ebi.ac.uk/pdbsum/8ho5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ho5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FCLN_PLAF7 FCLN_PLAF7] In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:17074076). In the apicoplast, degrades apicoplast transit peptides after their cleavage (PubMed:17074076). Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (By similarity). At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (By similarity). At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (By similarity). The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (By similarity).[UniProtKB:A0A0L7KF24]<ref>PMID:17074076</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Plasmodium falciparum 3D7]] | ||
| + | [[Category: Chung Z]] | ||
| + | [[Category: Lescar J]] | ||
| + | [[Category: Lin JQ]] | ||
Revision as of 10:01, 20 December 2023
Falcilysin in complex with MMV665806
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