3pmn
From Proteopedia
(Difference between revisions)
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:3pmn.png|left|200px]] | ||
| - | + | ==ternary crystal structure of polymerase lambda variant with a GT mispair at the primer terminus with Mn2+ in the active site== | |
| - | + | <StructureSection load='3pmn' size='340' side='right'caption='[[3pmn]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3pmn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PMN 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]] 2.2Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1GC:2-DEOXY-5-O-[(R)-HYDROXY{[(S)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]METHYL}PHOSPHORYL]GUANOSINE'>1GC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=3pmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pmn OCA], [https://pdbe.org/3pmn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pmn RCSB], [https://www.ebi.ac.uk/pdbsum/3pmn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pmn ProSAT]</span></td></tr> |
| - | [[3pmn]] is a 4 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DPOLL_HUMAN DPOLL_HUMAN] Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.<ref>PMID:11457865</ref> <ref>PMID:15537631</ref> | ||
==See Also== | ==See Also== | ||
| - | *[[DNA polymerase|DNA polymerase]] | + | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Bebenek K]] |
| - | [[Category: | + | [[Category: Kunkel TA]] |
| - | [[Category: | + | [[Category: Pedersen LC]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
ternary crystal structure of polymerase lambda variant with a GT mispair at the primer terminus with Mn2+ in the active site
| |||||||||||
