Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009236 | biological_process | cobalamin biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0043755 | molecular_function | alpha-ribazole phosphatase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009236 | biological_process | cobalamin biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0043755 | molecular_function | alpha-ribazole phosphatase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009236 | biological_process | cobalamin biosynthetic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016791 | molecular_function | phosphatase activity |
| C | 0043755 | molecular_function | alpha-ribazole phosphatase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009236 | biological_process | cobalamin biosynthetic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016791 | molecular_function | phosphatase activity |
| D | 0043755 | molecular_function | alpha-ribazole phosphatase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | PRO24 |
| A | THR25 |
| A | ARG57 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | ARG7 |
| A | ASN14 |
| A | HOH410 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue 1PE A 303 |
| Chain | Residue |
| A | GLN139 |
| A | LYS186 |
| A | ILE132 |
| A | ALA133 |
| A | SER136 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue 1PE A 304 |
| Chain | Residue |
| A | GLU81 |
| A | MET82 |
| A | PHE84 |
| A | CYS107 |
| A | MET168 |
| A | TRP169 |
| A | HOH430 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 301 |
| Chain | Residue |
| B | PRO24 |
| B | THR25 |
| B | GLU56 |
| B | ARG57 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | GLU81 |
| B | MET82 |
| B | TRP169 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LiRHGEtQaN |
| Chain | Residue | Details |
| A | LEU5-ASN14 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"UniProtKB","id":"P62707","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P62707","evidenceCode":"ECO:0000250"}]} |
