5y1k: Difference between revisions

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<StructureSection load='5y1k' size='340' side='right'caption='[[5y1k]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
<StructureSection load='5y1k' size='340' side='right'caption='[[5y1k]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5y1k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plafq Plafq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y1K FirstGlance]. <br>
<table><tr><td colspan='2'>[[5y1k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_FcB1/Columbia Plasmodium falciparum FcB1/Columbia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y1K FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1B:(2S)-2-[(2-chlorophenyl)methylcarbamoylamino]-4-methyl-N-oxidanyl-pentanamide'>B1B</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1B:(2S)-2-[(2-chlorophenyl)methylcarbamoylamino]-4-methyl-N-oxidanyl-pentanamide'>B1B</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5y1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1k OCA], [https://pdbe.org/5y1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y1k RCSB], [https://www.ebi.ac.uk/pdbsum/5y1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1k 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=5y1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1k OCA], [https://pdbe.org/5y1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y1k RCSB], [https://www.ebi.ac.uk/pdbsum/5y1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1k ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/AMP1_PLAFQ AMP1_PLAFQ]] Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC.<ref>PMID:12166515</ref> <ref>PMID:19196988</ref>
[https://www.uniprot.org/uniprot/AMP1_PLAFQ AMP1_PLAFQ] Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC.<ref>PMID:12166515</ref> <ref>PMID:19196988</ref>  


==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Plafq]]
[[Category: Plasmodium falciparum FcB1/Columbia]]
[[Category: Addlagatta, A]]
[[Category: Addlagatta A]]
[[Category: Marapaka, A K]]
[[Category: Marapaka AK]]
[[Category: Zhang, Y]]
[[Category: Zhang Y]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: M1-class aminopeptidase]]

Latest revision as of 11:19, 22 November 2023

Crystal structure of Plasmodium falciparum aminopeptidase N in complex with (S)-2-(3-(2-chlorobenzyl)ureido)-N-hydroxy-4-methylpentanamideCrystal structure of Plasmodium falciparum aminopeptidase N in complex with (S)-2-(3-(2-chlorobenzyl)ureido)-N-hydroxy-4-methylpentanamide

Structural highlights

5y1k is a 1 chain structure with sequence from Plasmodium falciparum FcB1/Columbia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.81Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMP1_PLAFQ Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC.[1] [2]

See Also

References

  1. ↑ Allary M, Schrevel J, Florent I. Properties, stage-dependent expression and localization of Plasmodium falciparum M1 family zinc-aminopeptidase. Parasitology. 2002 Jul;125(Pt 1):1-10. PMID:12166515
  2. ↑ McGowan S, Porter CJ, Lowther J, Stack CM, Golding SJ, Skinner-Adams TS, Trenholme KR, Teuscher F, Donnelly SM, Grembecka J, Mucha A, Kafarski P, Degori R, Buckle AM, Gardiner DL, Whisstock JC, Dalton JP. Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase. Proc Natl Acad Sci U S A. 2009 Feb 5. PMID:19196988

5y1k, resolution 1.81Å

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