1IMF
STRUCTURAL STUDIES OF METAL BINDING BY INOSITOL MONOPHOSPHATASE: EVIDENCE FOR TWO-METAL ION CATALYSIS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004346 | molecular_function | glucose-6-phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006020 | biological_process | inositol metabolic process |
| A | 0006021 | biological_process | inositol biosynthetic process |
| A | 0006661 | biological_process | phosphatidylinositol biosynthetic process |
| A | 0006796 | biological_process | phosphate-containing compound metabolic process |
| A | 0007165 | biological_process | signal transduction |
| A | 0008877 | molecular_function | glucose-1-phosphatase activity |
| A | 0008934 | molecular_function | inositol monophosphate 1-phosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0031403 | molecular_function | lithium ion binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047954 | molecular_function | glycerol-2-phosphatase activity |
| A | 0052832 | molecular_function | inositol monophosphate 3-phosphatase activity |
| A | 0052833 | molecular_function | inositol monophosphate 4-phosphatase activity |
| A | 0052834 | molecular_function | inositol monophosphate phosphatase activity |
| A | 0103026 | molecular_function | fructose-1-phosphatase activity |
Functional Information from PDB Data
| site_id | M1 |
| Number of Residues | 8 |
| Details | ACTIVE SITE |
| Chain | Residue |
| A | GLU70 |
| A | ASP90 |
| A | PRO91 |
| A | ILE92 |
| A | ASP93 |
| A | GLY94 |
| A | THR95 |
| A | ASP220 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8068620, ECO:0000303|PubMed:8068621 |
| Chain | Residue | Details |
| A | GLU70 | |
| A | GLU213 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068621 |
| Chain | Residue | Details |
| A | ASP90 | |
| A | ASP93 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23027737, ECO:0000269|PubMed:8068621, ECO:0000303|PubMed:1332026, ECO:0000303|PubMed:8068620 |
| Chain | Residue | Details |
| A | ILE92 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8068620 |
| Chain | Residue | Details |
| A | GLY194 | |
| A | ASP220 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR168 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ima |
| Chain | Residue | Details |
| A | THR95 | |
| A | GLU70 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 577 |
| Chain | Residue | Details |
| A | GLU70 | metal ligand, proton acceptor, proton donor |
| A | ASP90 | metal ligand |
| A | ILE92 | metal ligand |
| A | ASP93 | metal ligand |
| A | THR95 | hydrogen bond acceptor |
| A | ASP220 | metal ligand |
