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PDBe Entry: 1imd 
STRUCTURAL STUDIES OF METAL BINDING BY INOSITOL MONOPHOSPHATASE: EVIDENCE FOR TWO-METAL ION CATALYSIS
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HYDROLASE
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X-RAY DIFFRACTION
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Resolution: 2.6 Å, R-factor: 18.8%, Spacegroup: P 32 2 1
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27/02/1995, deposition: 08/02/1994, last revision: 24/02/2009
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Bone, R.
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Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis.
BIOCHEMISTRY vol:33, pag:9468-9476 (1994) [PubMed ID 8068621 ]
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HYDROLASE
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3.1.3.25 ExPASy BRENDA (A B)
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Homo sapiens(human) 9606(A B)
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Inositol monophosphatase (EC 3.1.3.25) (Inositol-1(or 4)-monophosphatase) (IMPase) (IMP) (Lithium-sensitive myo-inositol monophosphatase A1) P29218 (A B)
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A, B
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| A, B |
INOSITOL MONOPHOSPHATASE |
Protein |
P29218 (IMPA1_HUMAN)
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277 |
98% |
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| A, B |
MANGANESE (II) ION |
MN
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| A, B |
PHOSPHATE ION |
PO4
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