2bwg: Difference between revisions

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<StructureSection load='2bwg' size='340' side='right'caption='[[2bwg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='2bwg' size='340' side='right'caption='[[2bwg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2bwg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BWG FirstGlance]. <br>
<table><tr><td colspan='2'>[[2bwg]] 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=2BWG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BWG FirstGlance]. <br>
</td></tr><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=K:POTASSIUM+ION'>K</scene></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]] 2.4&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ble|2ble]]</div></td></tr>
<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=K:POTASSIUM+ION'>K</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/GMP_reductase GMP reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.1.7 1.7.1.7] </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=2bwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bwg OCA], [https://pdbe.org/2bwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bwg RCSB], [https://www.ebi.ac.uk/pdbsum/2bwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bwg ProSAT]</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=2bwg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bwg OCA], [https://pdbe.org/2bwg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bwg RCSB], [https://www.ebi.ac.uk/pdbsum/2bwg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bwg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: GMP reductase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[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: Nucleotide pathway]]
[[Category: Oxidoreductase]]
[[Category: Tim barrel]]

Latest revision as of 16:57, 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

2bwg is a 4 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 2.4Å
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

2bwg, resolution 2.40Å

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