1G0I
CRYSTAL STRUCTURE OF MJ0109 GENE PRODUCT INOSITOL MONOPHOSPHATASE-FRUCTOSE 1,6 BISPHOSPHATASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006020 | biological_process | inositol metabolic process |
A | 0007165 | biological_process | signal transduction |
A | 0008934 | molecular_function | inositol monophosphate 1-phosphatase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
A | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
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 |
B | 0006020 | biological_process | inositol metabolic process |
B | 0007165 | biological_process | signal transduction |
B | 0008934 | molecular_function | inositol monophosphate 1-phosphatase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
B | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0052832 | molecular_function | inositol monophosphate 3-phosphatase activity |
B | 0052833 | molecular_function | inositol monophosphate 4-phosphatase activity |
B | 0052834 | molecular_function | inositol monophosphate phosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 290 |
Chain | Residue |
A | ASP81 |
A | ASP84 |
A | ASP201 |
A | MN291 |
A | PO4293 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 291 |
Chain | Residue |
A | PO4293 |
A | HOH635 |
A | GLU65 |
A | ASP81 |
A | ILE83 |
A | MN290 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN A 292 |
Chain | Residue |
A | ASP38 |
A | GLU65 |
A | PO4293 |
A | HOH634 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 A 293 |
Chain | Residue |
A | GLU65 |
A | ASP81 |
A | ILE83 |
A | ASP84 |
A | GLY85 |
A | SER86 |
A | ARG198 |
A | ASP201 |
A | MN290 |
A | MN291 |
A | MN292 |
A | HOH634 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 590 |
Chain | Residue |
B | GLU365 |
B | ASP381 |
B | ILE383 |
B | PO4593 |
B | HOH644 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 591 |
Chain | Residue |
B | GLU365 |
B | ASP381 |
B | ASP384 |
B | ASP501 |
B | PO4593 |
B | HOH629 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 592 |
Chain | Residue |
B | ASP338 |
B | GLU365 |
B | ARG498 |
B | PO4593 |
B | HOH645 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PO4 B 593 |
Chain | Residue |
B | GLU365 |
B | ASP381 |
B | ILE383 |
B | ASP384 |
B | GLY385 |
B | SER386 |
B | ARG498 |
B | MN590 |
B | MN591 |
B | MN592 |
B | HOH645 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE INS B 294 |
Chain | Residue |
A | GLY173 |
B | LYS467 |
B | ARG468 |
B | VAL469 |
B | ARG470 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE INS A 594 |
Chain | Residue |
A | ARG168 |
A | ARG170 |
B | TYR452 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11062561, ECO:0000305|PubMed:11170378 |
Chain | Residue | Details |
A | GLU65 | |
B | ASP501 | |
A | ASP81 | |
A | ILE83 | |
A | ASP84 | |
A | ASP201 | |
B | GLU365 | |
B | ASP381 | |
B | ILE383 | |
B | ASP384 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11170378 |
Chain | Residue | Details |
A | ARG170 | |
A | PHE175 | |
A | ARG194 | |
B | ARG470 | |
B | PHE475 | |
B | ARG494 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eyi |
Chain | Residue | Details |
A | ASP38 | |
A | ASP44 | |
A | GLU66 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eyi |
Chain | Residue | Details |
B | ASP338 | |
B | GLU366 | |
B | ASP344 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eyi |
Chain | Residue | Details |
A | SER86 | |
A | GLU65 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eyi |
Chain | Residue | Details |
B | SER386 | |
B | GLU365 |