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 |