2ble: Difference between revisions

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<StructureSection load='2ble' size='340' side='right'caption='[[2ble]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2ble' size='340' side='right'caption='[[2ble]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2ble]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BLE FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ble FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ble OCA], [http://pdbe.org/2ble PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ble RCSB], [http://www.ebi.ac.uk/pdbsum/2ble PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ble 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=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>
</table>
== 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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
== References ==
<references/>
__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 16:43, 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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