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[[Image:2ble.gif|left|200px]]


{{Structure
==Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP==
|PDB= 2ble |SIZE=350|CAPTION= <scene name='initialview01'>2ble</scene>, resolution 1.90&Aring;
<StructureSection load='2ble' size='340' side='right'caption='[[2ble]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Na+Binding+Site+For+Chain+A'>AC1</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=5GP:GUANOSINE-5&#39;-MONOPHOSPHATE'>5GP</scene>
<table><tr><td colspan='2'>[[2ble]] is a 1 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=2BLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BLE FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/GMP_reductase GMP reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.7 1.7.1.7]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</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=2ble FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ble OCA], [https://pdbe.org/2ble PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ble RCSB], [https://www.ebi.ac.uk/pdbsum/2ble PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ble ProSAT]</span></td></tr>
 
</table>
'''STRUCTURE OF HUMAN GUANOSINE MONOPHOSPHATE REDUCTASE GMPR1 IN COMPLEX WITH GMP'''
== Function ==
 
[https://www.uniprot.org/uniprot/GMPR1_HUMAN GMPR1_HUMAN] Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.<ref>PMID:1694726</ref>
 
== Evolutionary Conservation ==
==About this Structure==
[[Image:Consurf_key_small.gif|200px|right]]
2BLE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BLE OCA].  
Check<jmol>
[[Category: GMP reductase]]
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bl/2ble_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ble ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C.]]
[[Category: Arrowsmith C]]
[[Category: Bunkoczi, G.]]
[[Category: Bunkoczi G]]
[[Category: Delft, F Von.]]
[[Category: Edwards A]]
[[Category: Edwards, A.]]
[[Category: Gileadi O]]
[[Category: Gileadi, O.]]
[[Category: Haroniti A]]
[[Category: Haroniti, A.]]
[[Category: Ng S]]
[[Category: Ng, S.]]
[[Category: Oppermann U]]
[[Category: Oppermann, U.]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M.]]
[[Category: Von Delft F]]
[[Category: 5GP]]
[[Category: NA]]
[[Category: nucleotide pathway]]
[[Category: tim barrel]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:45:55 2008''

Latest revision as of 16:43, 13 December 2023

Structure of human guanosine monophosphate reductase GMPR1 in complex with GMPStructure of human guanosine monophosphate reductase GMPR1 in complex with GMP

Structural highlights

2ble is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GMPR1_HUMAN Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.[1]

Evolutionary Conservation

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

References

  1. ↑ Yoshida A, Kan YW. Origin of "fused" glucose-6-phosphate dehydrogenase. Cell. 1990 Jul 13;62(1):11-2. PMID:1694726

2ble, resolution 1.90Å

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