4q2h: Difference between revisions

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'''Unreleased structure'''


The entry 4q2h is ON HOLD
==Crystal structure of probable proline racemase from agrobacterium radiobacter K84, TARGET EFI-506561, with bound carbonate==
 
<StructureSection load='4q2h' size='340' side='right'caption='[[4q2h]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
Authors: Patskovsky, Y., Toro, R., Bhosle, R., Al Obaidi, N.F., Morisco, L.L., Wasserman, S.R., Sojitra, S., Stead, M., Washington, E., Glenn, A.S., Chowdhury, S., Evans, B., Hammonds, J., Hillerich, B., Love, J., Seidel, R.D., Gerlt, J.A., Almo, S.C., Enzyme Function Initiative (Efi)
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4q2h]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_radiobacter_K84 Agrobacterium radiobacter K84]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q2H FirstGlance]. <br>
Description: CRYSTAL STRUCTURE OF PROBABLE PROLINE RACEMASE FROM AGROBACTERIUM RADIOBACTER K84, TARGET EFI-506561, WITH BOUND CARBONATE
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4q2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2h OCA], [https://pdbe.org/4q2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q2h RCSB], [https://www.ebi.ac.uk/pdbsum/4q2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q2h ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/4HPE1_RHIR8 4HPE1_RHIR8] Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. Displays no proline racemase activity.<ref>PMID:24980702</ref>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Agrobacterium radiobacter K84]]
[[Category: Large Structures]]
[[Category: Al Obaidi NF]]
[[Category: Almo SC]]
[[Category: Bhosle R]]
[[Category: Chowdhury S]]
[[Category: Evans B]]
[[Category: Gerlt JA]]
[[Category: Glenn AS]]
[[Category: Hammonds J]]
[[Category: Hillerich B]]
[[Category: Love J]]
[[Category: Morisco LL]]
[[Category: Patskovsky Y]]
[[Category: Seidel RD]]
[[Category: Sojitra S]]
[[Category: Stead M]]
[[Category: Toro R]]
[[Category: Washington E]]
[[Category: Wasserman SR]]

Latest revision as of 13:26, 30 October 2024

Crystal structure of probable proline racemase from agrobacterium radiobacter K84, TARGET EFI-506561, with bound carbonateCrystal structure of probable proline racemase from agrobacterium radiobacter K84, TARGET EFI-506561, with bound carbonate

Structural highlights

4q2h is a 2 chain structure with sequence from Agrobacterium radiobacter K84. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

4HPE1_RHIR8 Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. Displays no proline racemase activity.[1]

References

  1. ↑ Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP. Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. Elife. 2014 Jun 30;3. doi: 10.7554/eLife.03275. PMID:24980702 doi:http://dx.doi.org/10.7554/eLife.03275

4q2h, resolution 1.80Å

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