4fo4: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP and mycophenolic acid== | |||
<StructureSection load='4fo4' size='340' side='right'caption='[[4fo4]], [[Resolution|resolution]] 2.03Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fo4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FO4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.03Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MOA:MYCOPHENOLIC+ACID'>MOA</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=4fo4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fo4 OCA], [https://pdbe.org/4fo4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fo4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fo4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fo4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9KTW3_VIBCH Q9KTW3_VIBCH] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (By similarity).[HAMAP-Rule:MF_01964] | |||
== | ==See Also== | ||
*[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[ | [[Category: Large Structures]] | ||
[[Category: | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] | ||
[[Category: Vibrio cholerae | [[Category: Anderson WF]] | ||
[[Category: Anderson | [[Category: Gu M]] | ||
[[Category: Joachimiak A]] | |||
[[Category: Gu | [[Category: Makowska-Grzyska M]] | ||
[[Category: Joachimiak | [[Category: Maltseva N]] | ||
[[Category: Makowska-Grzyska | [[Category: Osipiuk J]] | ||
[[Category: Maltseva | |||
[[Category: Osipiuk | |||
Latest revision as of 18:30, 14 March 2024
Inosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP and mycophenolic acidInosine 5'-monophosphate dehydrogenase from Vibrio cholerae, deletion mutant, complexed with IMP and mycophenolic acid
Structural highlights
FunctionQ9KTW3_VIBCH Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (By similarity).[HAMAP-Rule:MF_01964] See Also |
| ||||||||||||||||||