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5hp4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure bacteriohage T5 D15 flap endonuclease (D155K) pseudo-enzyme-product complex with DNA and metal ions== | |
| - | + | <StructureSection load='5hp4' size='340' side='right' caption='[[5hp4]], [[Resolution|resolution]] 1.86Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5hp4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HP4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HP4 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hnk|5hnk]]</td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exodeoxyribonuclease_(lambda-induced) Exodeoxyribonuclease (lambda-induced)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.3 3.1.11.3] </span></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=5hp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hp4 OCA], [http://pdbe.org/5hp4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hp4 RCSB], [http://www.ebi.ac.uk/pdbsum/5hp4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/EXO5_BPT5 EXO5_BPT5]] 5'-exonucleolytic degradation of double-stranded (ds) DNA. Can also cleave bifurcated nucleic acids such as flap and pseudo-Y substrates in a structure-specific manner. This requires free 5' single-stranded (ss) ends and cleaves at the ds/ss junction. Binds DNA pseudo-Y substrates with a dissociation constant of 5 nM. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Almalki, F A]] | ||
| + | [[Category: Artymiuk, P A]] | ||
| + | [[Category: Rafferty, J B]] | ||
| + | [[Category: Sayers, J R]] | ||
| + | [[Category: Sedelnikova, S E]] | ||
| + | [[Category: Zhang, J]] | ||
| + | [[Category: Enzyme-substrate-complex]] | ||
| + | [[Category: Flap endonuclease]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Metalloenzyme]] | ||
Revision as of 06:09, 2 June 2016
Crystal structure bacteriohage T5 D15 flap endonuclease (D155K) pseudo-enzyme-product complex with DNA and metal ions
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