Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004441 | molecular_function | inositol-1,4-bisphosphate 1-phosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052829 | molecular_function | inositol-1,3,4-trisphosphate 1-phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | ASP317 |
| A | ASP153 |
| A | ASP156 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | ASP54 |
| A | GLU79 |
| A | ASP153 |
| A | ILE155 |
| A | THR158 |
| site_id | MAG |
| Number of Residues | 7 |
| Details | |
| Chain | Residue |
| A | ASP54 |
| A | GLU79 |
| A | GLU80 |
| A | ASP153 |
| A | ASP156 |
| A | ASP317 |
| A | HOH447 |
Functional Information from PROSITE/UniProt
| site_id | PS00629 |
| Number of Residues | 13 |
| Details | IMP_1 Inositol monophosphatase family signature 1. W.VDPIDSTyqYiK |
| Chain | Residue | Details |
| A | TRP151-LYS163 | |
| site_id | PS00630 |
| Number of Residues | 15 |
| Details | IMP_2 Inositol monophosphatase family signature 2. WDsCAAhAILramGG |
| Chain | Residue | Details |
| A | TRP316-GLY330 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 19 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33172890","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7947723","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1INP","evidenceCode":"ECO:0000312"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33172890","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7KIR","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P49441","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 856 |
| Chain | Residue | Details |
| A | ASP54 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLU79 | metal ligand |
| A | ASP153 | metal ligand |
| A | ILE155 | metal ligand |
| A | ASP156 | metal ligand |
| A | THR158 | electrostatic stabiliser, enhance reactivity, increase nucleophilicity, proton acceptor, proton donor, proton relay |
| A | ASP317 | metal ligand |
