3v9i: Difference between revisions

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[[Image:3v9i.jpg|left|200px]]


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==Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352L==
The line below this paragraph, containing "STRUCTURE_3v9i", creates the "Structure Box" on the page.
<StructureSection load='3v9i' size='340' side='right'caption='[[3v9i]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3v9i]] 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=3V9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V9I FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v9i OCA], [https://pdbe.org/3v9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v9i RCSB], [https://www.ebi.ac.uk/pdbsum/3v9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v9i ProSAT]</span></td></tr>
{{STRUCTURE_3v9i|  PDB=3v9i  |  SCENE=  }}
</table>
== Disease ==
[https://www.uniprot.org/uniprot/AL4A1_HUMAN AL4A1_HUMAN] Hyperprolinemia type 2. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/AL4A1_HUMAN AL4A1_HUMAN] Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes.<ref>PMID:22516612</ref>  


===Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352L===
==See Also==
 
*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
 
*[[Pyrroline-5-carboxylate dehydrogenase|Pyrroline-5-carboxylate dehydrogenase]]
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== References ==
The line below this paragraph, {{ABSTRACT_PUBMED_22516612}}, adds the Publication Abstract to the page
<references/>
(as it appears on PubMed at http://www.pubmed.gov), where 22516612 is the PubMed ID number.
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</StructureSection>
{{ABSTRACT_PUBMED_22516612}}
 
==About this Structure==
[[3v9i]] is a 4 chain structure with 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=3V9I OCA].
 
==Reference==
<ref group="xtra">PMID:022516612</ref><references group="xtra"/>
[[Category: 1-pyrroline-5-carboxylate dehydrogenase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Singh, R K.]]
[[Category: Large Structures]]
[[Category: Tanner, J J.]]
[[Category: Singh RK]]
[[Category: Acting on aldehyde or oxo group of donor]]
[[Category: Tanner JJ]]
[[Category: Aldehyde dehydrogenase]]
[[Category: Mitochondria]]
[[Category: Nad or nadp as acceptor]]
[[Category: Nucleotide binding]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]

Latest revision as of 17:21, 14 March 2024

Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352LCrystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant S352L

Structural highlights

3v9i 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 2.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

AL4A1_HUMAN Hyperprolinemia type 2. The disease is caused by mutations affecting the gene represented in this entry.

Function

AL4A1_HUMAN Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes.[1]

See Also

References

  1. ↑ Srivastava D, Singh RK, Moxley MA, Henzl MT, Becker DF, Tanner JJ. The Three-Dimensional Structural Basis of Type II Hyperprolinemia. J Mol Biol. 2012 Apr 16. PMID:22516612 doi:10.1016/j.jmb.2012.04.010

3v9i, resolution 2.85Å

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