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6jgu
From Proteopedia
(Difference between revisions)
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==Crystal structure at atomic resolution reveals the catalytic mechanism in peptidyl-tRNA hydrolase from Acinetobacter baumannii.== | ==Crystal structure at atomic resolution reveals the catalytic mechanism in peptidyl-tRNA hydrolase from Acinetobacter baumannii.== | ||
| - | <StructureSection load='6jgu' size='340' side='right' | + | <StructureSection load='6jgu' size='340' side='right'caption='[[6jgu]], [[Resolution|resolution]] 1.02Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6jgu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JGU OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6jgu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_ATCC_19606_=_CIP_70.34_=_JCM_6841 Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JGU FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.02Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jgu OCA], [https://pdbe.org/6jgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jgu RCSB], [https://www.ebi.ac.uk/pdbsum/6jgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jgu ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/D0C9L6_ACIB2 D0C9L6_ACIB2] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.[HAMAP-Rule:MF_00083] |
| + | |||
| + | ==See Also== | ||
| + | *[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Acinetobacter baumannii ATCC 19606 = CIP 70 34 = JCM 6841]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Sharma | + | [[Category: Sharma P]] |
| - | [[Category: | + | [[Category: Sharma S]] |
| - | [[Category: | + | [[Category: Singh TP]] |
| - | [[Category: | + | [[Category: Viswanathan V]] |
Current revision
Crystal structure at atomic resolution reveals the catalytic mechanism in peptidyl-tRNA hydrolase from Acinetobacter baumannii.
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