1LBX
Crystal Structure of a ternary complex of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus with Calcium ions and D-myo-Inositol-1-Phosphate
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 | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 290 |
| Chain | Residue |
| A | ASP82 |
| A | ASP85 |
| A | ASP200 |
| A | IPD295 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 291 |
| Chain | Residue |
| A | GLU67 |
| A | ASP82 |
| A | LEU84 |
| A | IPD295 |
| A | HOH1077 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 590 |
| Chain | Residue |
| B | GLU367 |
| B | ASP382 |
| B | LEU384 |
| B | CA591 |
| B | IPD595 |
| B | HOH1088 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 591 |
| Chain | Residue |
| B | GLU367 |
| B | ASP382 |
| B | ASP385 |
| B | ASP500 |
| B | CA590 |
| B | IPD595 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IPD A 295 |
| Chain | Residue |
| A | GLU67 |
| A | ASP82 |
| A | LEU84 |
| A | ASP85 |
| A | GLY86 |
| A | THR87 |
| A | TYR155 |
| A | GLY170 |
| A | SER171 |
| A | ALA172 |
| A | GLU175 |
| A | ASP200 |
| A | CA290 |
| A | CA291 |
| A | HOH1029 |
| A | HOH1077 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE IPD B 595 |
| Chain | Residue |
| B | GLU367 |
| B | ASP385 |
| B | GLY386 |
| B | THR387 |
| B | TYR455 |
| B | GLY470 |
| B | SER471 |
| B | ALA472 |
| B | ARG491 |
| B | MET495 |
| B | ASP500 |
| B | CA590 |
| B | CA591 |
| B | HOH1041 |
| B | HOH1091 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP38 | |
| A | ASP200 | |
| B | ASP338 | |
| B | THR340 | |
| B | GLU367 | |
| B | ASP382 | |
| B | LEU384 | |
| B | ASP385 | |
| B | ARG467 | |
| B | ALA472 | |
| B | ARG491 | |
| A | THR40 | |
| B | ASP500 | |
| A | GLU67 | |
| A | ASP82 | |
| A | LEU84 | |
| A | ASP85 | |
| A | ARG167 | |
| A | ALA172 | |
| A | ARG191 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ima |
| Chain | Residue | Details |
| A | THR87 | |
| A | GLU67 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ima |
| Chain | Residue | Details |
| B | GLU367 | |
| B | THR387 |
