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New page: '''Unreleased structure''' The entry 4jbd is ON HOLD Authors: Vetting, M.W., Toro, R., Bhosle, R., Al Obaidi, N.F., Morisco, L.L., Wasserman, S.R., Sojitra, S., Washington, E., Scott Gl... |
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==Crystal structure of Pput_1285, a putative hydroxyproline epimerase from Pseudomonas putida f1 (target EFI-506500), open form, space group I2, bound citrate== | |||
<StructureSection load='4jbd' size='340' side='right'caption='[[4jbd]], [[Resolution|resolution]] 1.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jbd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_F1 Pseudomonas putida F1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JBD 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]] 1.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=4jbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jbd OCA], [https://pdbe.org/4jbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jbd RCSB], [https://www.ebi.ac.uk/pdbsum/4jbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jbd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/4HYPE_PSEP1 4HYPE_PSEP1] Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with 200-fold lower efficiency.<ref>PMID:24980702</ref> | |||
==See Also== | |||
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas putida F1]] | |||
[[Category: Al Obaidi NF]] | |||
[[Category: Almo SC]] | |||
[[Category: Bhosle R]] | |||
[[Category: Chowdhury S]] | |||
[[Category: Evans B]] | |||
[[Category: Gerlt JA]] | |||
[[Category: Hammonds J]] | |||
[[Category: Hillerich B]] | |||
[[Category: Imker HJ]] | |||
[[Category: Love J]] | |||
[[Category: Morisco LL]] | |||
[[Category: Scott Glenn A]] | |||
[[Category: Seidel RD]] | |||
[[Category: Sojitra S]] | |||
[[Category: Stead M]] | |||
[[Category: Toro R]] | |||
[[Category: Vetting MW]] | |||
[[Category: Washington E]] | |||
[[Category: Wasserman SR]] |
Latest revision as of 18:39, 20 September 2023
Crystal structure of Pput_1285, a putative hydroxyproline epimerase from Pseudomonas putida f1 (target EFI-506500), open form, space group I2, bound citrateCrystal structure of Pput_1285, a putative hydroxyproline epimerase from Pseudomonas putida f1 (target EFI-506500), open form, space group I2, bound citrate
Structural highlights
Function4HYPE_PSEP1 Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with 200-fold lower efficiency.[1] See AlsoReferences
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