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==Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound zn, space group c2==
==Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound zn, space group c2==
<StructureSection load='4do7' size='340' side='right' caption='[[4do7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4do7' size='340' side='right'caption='[[4do7]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4do7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Burm1 Burm1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DO7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4do7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_multivorans_ATCC_17616 Burkholderia multivorans ATCC 17616]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DO7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bmul_3602, BMULJ_04915 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=395019 BURM1])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4do7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do7 OCA], [http://pdbe.org/4do7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4do7 RCSB], [http://www.ebi.ac.uk/pdbsum/4do7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4do7 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=4do7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4do7 OCA], [https://pdbe.org/4do7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4do7 RCSB], [https://www.ebi.ac.uk/pdbsum/4do7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4do7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FCNLN_BURM1 FCNLN_BURM1] L-fucono-1,5-lactonase involved in an L-fucose degradation pathway (PubMed:23214453). Catalyzes the hydrolysis of L-fucono-1,5-lactone to L-fuconate (PubMed:23214453). L-fucono-1,5-lactone is the best substrate, but the enzyme can also hydrolyze L-fucono-1,4-lactone, L-galactono-1,4-lactone D-arabinono-1,4-lactone and L-xylono-1,4-lactone (PubMed:23214453).<ref>PMID:23214453</ref>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Burm1]]
[[Category: Burkholderia multivorans ATCC 17616]]
[[Category: Almo, S C]]
[[Category: Large Structures]]
[[Category: Bhosle, R]]
[[Category: Al Obaidi NF]]
[[Category: Chowdhury, S]]
[[Category: Almo SC]]
[[Category: EFI, Enzyme Function Initiative]]
[[Category: Bhosle R]]
[[Category: Evans, B]]
[[Category: Chowdhury S]]
[[Category: Gerlt, J A]]
[[Category: Evans B]]
[[Category: Glenn, A Scott]]
[[Category: Gerlt JA]]
[[Category: Hammonds, J]]
[[Category: Hammonds J]]
[[Category: Hillerich, B]]
[[Category: Hillerich B]]
[[Category: Imker, H J]]
[[Category: Imker HJ]]
[[Category: Morisco, L L]]
[[Category: Morisco LL]]
[[Category: Obaidi, N F.Al]]
[[Category: Raushel FM]]
[[Category: Raushel, F M]]
[[Category: Scott Glenn A]]
[[Category: Seidel, R D]]
[[Category: Seidel RD]]
[[Category: Sojitra, S]]
[[Category: Sojitra S]]
[[Category: Toro, R]]
[[Category: Toro R]]
[[Category: Vetting, M W]]
[[Category: Vetting MW]]
[[Category: Washington, E]]
[[Category: Washington E]]
[[Category: Wasserman, S R]]
[[Category: Wasserman SR]]
[[Category: Zencheck, W D]]
[[Category: Zencheck WD]]
[[Category: Amidohydrolase]]
[[Category: Efi]]
[[Category: Enzyme function initiative]]
[[Category: Hydrolase]]
[[Category: Putative lactonase]]
[[Category: Structural genomic]]
[[Category: Tim-barrel fold]]

Latest revision as of 11:18, 9 October 2024

Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound zn, space group c2Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound zn, space group c2

Structural highlights

4do7 is a 2 chain structure with sequence from Burkholderia multivorans ATCC 17616. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FCNLN_BURM1 L-fucono-1,5-lactonase involved in an L-fucose degradation pathway (PubMed:23214453). Catalyzes the hydrolysis of L-fucono-1,5-lactone to L-fuconate (PubMed:23214453). L-fucono-1,5-lactone is the best substrate, but the enzyme can also hydrolyze L-fucono-1,4-lactone, L-galactono-1,4-lactone D-arabinono-1,4-lactone and L-xylono-1,4-lactone (PubMed:23214453).[1]

References

  1. ↑ Hobbs ME, Vetting M, Williams HJ, Narindoshvili T, Kebodeaux DM, Hillerich B, Seidel RD, Almo SC, Raushel FM. Discovery of an L-fucono-1,5-lactonase from cog3618 of the amidohydrolase superfamily. Biochemistry. 2013 Jan 8;52(1):239-53. PMID:23214453 doi:10.1021/bi3015554

4do7, resolution 1.70Å

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