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1f2t
From Proteopedia
(Difference between revisions)
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<StructureSection load='1f2t' size='340' side='right'caption='[[1f2t]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1f2t' size='340' side='right'caption='[[1f2t]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1f2t]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1f2t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2T FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2u|1f2u]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f2u|1f2u]]</div></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=1f2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2t OCA], [https://pdbe.org/1f2t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2t RCSB], [https://www.ebi.ac.uk/pdbsum/1f2t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2t ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/RAD50_PYRFU RAD50_PYRFU]] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 09:45, 21 July 2021
Crystal Structure of ATP-Free RAD50 ABC-ATPase
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