1z2p
From Proteopedia
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|PDB= 1z2p |SIZE=350|CAPTION= <scene name='initialview01'>1z2p</scene>, resolution 1.22Å | |PDB= 1z2p |SIZE=350|CAPTION= <scene name='initialview01'>1z2p</scene>, resolution 1.22Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=I3S:(1S,3S,4S)-1,3,4-TRIPHOSPHO-MYO-INOSITOL'>I3S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1z2n|1Z2N]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z2p OCA], [http://www.ebi.ac.uk/pdbsum/1z2p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z2p RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Miller, G J.]] | [[Category: Miller, G J.]] | ||
[[Category: Wilson, M P.]] | [[Category: Wilson, M P.]] | ||
| - | [[Category: ACP]] | ||
| - | [[Category: I3S]] | ||
| - | [[Category: MG]] | ||
[[Category: atp-grasp]] | [[Category: atp-grasp]] | ||
[[Category: inositol phosphate kinase]] | [[Category: inositol phosphate kinase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:28:13 2008'' |
Revision as of 22:28, 30 March 2008
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| , resolution 1.22Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1Z2N
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Inositol 1,3,4-trisphosphate 5/6-Kinase in complex with Mg2+/AMP-PCP/Ins(1,3,4)P3
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
1Z2P 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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