1mjf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:44, 14 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='1mjf' size='340' side='right'caption='[[1mjf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1mjf' size='340' side='right'caption='[[1mjf]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1mjf]] 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=1MJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJF FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1mjf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJF FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1inl|1inl]]</div></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.798&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Spermidine_synthase Spermidine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.16 2.5.1.16] </span></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=1mjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mjf OCA], [https://pdbe.org/1mjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mjf RCSB], [https://www.ebi.ac.uk/pdbsum/1mjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mjf ProSAT], [https://www.topsan.org/Proteins/SECSG/1mjf TOPSAN]</span></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=1mjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mjf OCA], [https://pdbe.org/1mjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mjf RCSB], [https://www.ebi.ac.uk/pdbsum/1mjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mjf ProSAT], [https://www.topsan.org/Proteins/SECSG/1mjf TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/SPEE_PYRFU SPEE_PYRFU]] Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to various amine acceptors such as cadaverine, putrescine, agmatine, 1,3-diaminopropane, and sym-nor-spermidine. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet.<ref>PMID:17545282</ref>
+
[https://www.uniprot.org/uniprot/SPEE_PYRFU SPEE_PYRFU] Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to various amine acceptors such as cadaverine, putrescine, agmatine, 1,3-diaminopropane, and sym-nor-spermidine. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet.<ref>PMID:17545282</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 27: Line 26:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 43587]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Spermidine synthase]]
 
-
[[Category: Structural genomic]]
 
-
[[Category: PSI, Protein structure initiative]]
 
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
-
[[Category: Secsg]]
 
-
[[Category: Spermidine synthetase]]
 
-
[[Category: Transferase]]
 

Current revision

PUTATIVE SPERMIDINE SYNTHETASE FROM PYROCOCCUS FURIOSUS PFU-132382

PDB ID 1mjf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools