1z2o

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|PDB= 1z2o |SIZE=350|CAPTION= <scene name='initialview01'>1z2o</scene>, resolution 1.24&Aring;
|PDB= 1z2o |SIZE=350|CAPTION= <scene name='initialview01'>1z2o</scene>, resolution 1.24&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=I4P:(1S,3R,4R,6S)-1,3,4,6-TETRAPKISPHOSPHATE'>I4P</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=I4P:(1S,3R,4R,6S)-1,3,4,6-TETRAPKISPHOSPHATE'>I4P</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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[[Category: inositol phosphate kinase]]
[[Category: inositol phosphate kinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:30:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:25:44 2008''

Revision as of 12:25, 23 March 2008

Image:1z2o.gif


PDB ID 1z2o

Drag the structure with the mouse to rotate
, resolution 1.24Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with mg2+/ADP/Ins(1,3,4,6)P4


Overview

Inositol hexakisphosphate and other inositol high polyphosphates have diverse and critical roles in eukaryotic regulatory pathways. Inositol 1,3,4-trisphosphate 5/6-kinase catalyzes the rate-limiting step in inositol high polyphosphate synthesis in animals. This multifunctional enzyme also has inositol 3,4,5,6-tetrakisphosphate 1-kinase and other activities. The structure of an archetypal family member, from Entamoeba histolytica, has been determined to 1.2 A resolution in binary and ternary complexes with nucleotide, substrate, and product. The structure reveals an ATP-grasp fold. The inositol ring faces ATP edge-on such that the 5- and 6-hydroxyl groups are nearly equidistant from the ATP gamma-phosphate in catalytically productive phosphoacceptor positions and explains the unusual dual site specificity of this kinase. Inositol tris- and tetrakisphosphates interact via three phosphate binding subsites and one solvent-exposed site that could in principle be occupied by 18 different substrates, explaining the mechanisms for the multiple specificities and catalytic activities of this enzyme.

About this Structure

1Z2O is a Single protein structure of sequence from Eukaryota. Full crystallographic information is available from OCA.

Reference

Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase., Miller GJ, Wilson MP, Majerus PW, Hurley JH, Mol Cell. 2005 Apr 15;18(2):201-12. PMID:15837423

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