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- PDB-2hhm: STRUCTURE OF INOSITOL MONOPHOSPHATASE, THE PUTATIVE TARGET OF LIT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hhm | ||||||
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Title | STRUCTURE OF INOSITOL MONOPHOSPHATASE, THE PUTATIVE TARGET OF LITHIUM THERAPY | ||||||
![]() | INOSITOL MONOPHOSPHATASE | ||||||
![]() | HYDROLASE | ||||||
Function / homology | ![]() D-galactose 1-phosphate phosphatase / inositol monophosphate phosphatase activity / Synthesis of IP2, IP, and Ins in the cytosol / lithium ion binding / inositol biosynthetic process / inositol-phosphate phosphatase / inositol monophosphate 3-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 1-phosphatase activity / inositol metabolic process ...D-galactose 1-phosphate phosphatase / inositol monophosphate phosphatase activity / Synthesis of IP2, IP, and Ins in the cytosol / lithium ion binding / inositol biosynthetic process / inositol-phosphate phosphatase / inositol monophosphate 3-phosphatase activity / inositol monophosphate 4-phosphatase activity / inositol monophosphate 1-phosphatase activity / inositol metabolic process / phosphatidylinositol biosynthetic process / phosphate-containing compound metabolic process / phosphatidylinositol phosphate biosynthetic process / manganese ion binding / magnesium ion binding / signal transduction / protein homodimerization activity / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Bone, R. | ||||||
![]() | ![]() Title: Structure of inositol monophosphatase, the putative target of lithium therapy. Authors: Bone, R. / Springer, J.P. / Atack, J.R. #1: ![]() Title: C/DNA Cloning of Human and Rat Brain Myo-Inositol Monophosphatase: Expression and Characterization of the Human Recombinant Enzyme Authors: Mcallister, G. / Whiting, P. / Hammond, E.A. / Knowles, M.R. / Atack, J.R. / Bailey, F.J. / Maigetter, R. / Ragan, C.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 120.9 KB | Display | ![]() |
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PDB format | ![]() | 94.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 389.1 KB | Display | ![]() |
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Full document | ![]() | 401.4 KB | Display | |
Data in XML | ![]() | 13.5 KB | Display | |
Data in CIF | ![]() | 21.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO A 186 AND PRO B 186 ARE CIS PROLINES. |
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Components
#1: Protein | Mass: 30088.582 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.26 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.8 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.6 Å / Num. obs: 19468 / % possible obs: 93.3 % / Num. measured all: 64631 / Rmerge(I) obs: 0.064 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Rfactor obs: 0.166 / Highest resolution: 2.1 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.1 Å
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Refinement | *PLUS Highest resolution: 2.6 Å / Rfactor obs: 0.166 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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