1fw7: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 1: Line 1:


==NMR STRUCTURE OF 15N-LABELED BARNASE==
==NMR STRUCTURE OF 15N-LABELED BARNASE==
<StructureSection load='1fw7' size='340' side='right'caption='[[1fw7]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1fw7' size='340' side='right'caption='[[1fw7]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fw7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FW7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fw7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FW7 FirstGlance]. <br>
</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=1fw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw7 OCA], [https://pdbe.org/1fw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fw7 RCSB], [https://www.ebi.ac.uk/pdbsum/1fw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fw7 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1fw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fw7 OCA], [https://pdbe.org/1fw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fw7 RCSB], [https://www.ebi.ac.uk/pdbsum/1fw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fw7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM]] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.  
[https://www.uniprot.org/uniprot/RNBR_BACAM RNBR_BACAM] Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 24: Line 25:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arseniev, A S]]
[[Category: Arseniev AS]]
[[Category: Kirpichnikov, M P]]
[[Category: Kirpichnikov MP]]
[[Category: Reibarkh, M Y]]
[[Category: Reibarkh MY]]
[[Category: Schulga, A A]]
[[Category: Schulga AA]]
[[Category: Vasilieva, L I]]
[[Category: Vasilieva LI]]
[[Category: Alpha-beta protein]]
[[Category: Hydrolase]]
[[Category: Ribonuclease]]

Latest revision as of 14:17, 27 March 2024

NMR STRUCTURE OF 15N-LABELED BARNASENMR STRUCTURE OF 15N-LABELED BARNASE

Structural highlights

1fw7 is a 1 chain structure with sequence from Bacillus amyloliquefaciens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNBR_BACAM Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA