1la2

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|GENE= INO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= INO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG1260 INO1], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam07994 NAD_binding_5]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG1260 INO1], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam07994 NAD_binding_5]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1la2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1la2 OCA], [http://www.ebi.ac.uk/pdbsum/1la2 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1la2 RCSB]</span>
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1la2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1la2 OCA], [http://www.ebi.ac.uk/pdbsum/1la2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1la2 RCSB]</span>
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[[Category: yeast]]
[[Category: yeast]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:55:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:12 2008''

Revision as of 19:00, 30 March 2008

Image:1la2.gif


PDB ID 1la2

Drag the structure with the mouse to rotate
, resolution 2.65Å
Ligands: ,
Gene: INO1 (Saccharomyces cerevisiae)
Activity: Inositol-3-phosphate synthase, with EC number 5.5.1.4
Domains: INO1, NAD_binding_5
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase


Overview

The New York Structural Genomics Research Consortium has targeted highly conserved but uncharacterized enzyme families for structure determination. As part of this effort, the 2.65-A crystal structure has been determined for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an essential enzyme that catalyzes critical steps in inositol biosynthesis. The structure determination of four independent monomers in the asymmetric unit (240 kDa) reveals atomic details and residue composition for the partially closed NAD-containing active sites in apo-configuration. The structure further reveals extensive interactions involved in tetrameric assembly of the enzyme complex.

About this Structure

1LA2 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase., Kniewel R, Buglino JA, Shen V, Chadha T, Beckwith A, Lima CD, J Struct Funct Genomics. 2002;2(3):129-34. PMID:12836703

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