Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue GGS A 401 |
| Chain | Residue |
| A | ASN103 |
| A | ASN220 |
| A | SER224 |
| A | ARG227 |
| A | GLU228 |
| A | LEU281 |
| A | TRP288 |
| A | ARG294 |
| A | TYR295 |
| A | MG402 |
| A | HOH505 |
| A | THR106 |
| A | HOH509 |
| A | HOH543 |
| A | HOH561 |
| A | HOH566 |
| A | HOH647 |
| A | PHE107 |
| A | ASP110 |
| A | PHE149 |
| A | ARG177 |
| A | ILE181 |
| A | GLY182 |
| A | TRP186 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASN220 |
| A | SER224 |
| A | GLU228 |
| A | GGS401 |
| A | HOH561 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | binding site for residue GGS B 401 |
| Chain | Residue |
| B | ASN103 |
| B | PHE107 |
| B | ASP110 |
| B | PHE149 |
| B | ARG177 |
| B | ILE181 |
| B | GLY182 |
| B | VAL183 |
| B | TRP186 |
| B | ASN220 |
| B | SER224 |
| B | ARG227 |
| B | GLU228 |
| B | LEU281 |
| B | ASN285 |
| B | ARG294 |
| B | TYR295 |
| B | MG402 |
| B | HOH501 |
| B | HOH508 |
| B | HOH514 |
| B | HOH526 |
| B | HOH593 |
| B | HOH597 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASN220 |
| B | SER224 |
| B | GLU228 |
| B | GGS401 |
| B | HOH526 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | binding site for residue GGS C 401 |
| Chain | Residue |
| C | ASN103 |
| C | ASP110 |
| C | ARG177 |
| C | ILE181 |
| C | GLY182 |
| C | TRP186 |
| C | ASN220 |
| C | SER224 |
| C | ARG227 |
| C | GLU228 |
| C | TRP288 |
| C | ARG294 |
| C | TYR295 |
| C | MG402 |
| C | HOH510 |
| C | HOH551 |
| C | HOH596 |
| C | HOH606 |
| C | HOH629 |
| C | HOH649 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 402 |
| Chain | Residue |
| C | ASN220 |
| C | SER224 |
| C | GLU228 |
| C | GGS401 |
| C | HOH551 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | binding site for residue GGS D 401 |
| Chain | Residue |
| D | HOH503 |
| D | HOH527 |
| D | HOH560 |
| D | HOH566 |
| D | HOH598 |
| D | HOH625 |
| D | HOH636 |
| D | ASN103 |
| D | PHE107 |
| D | ASP110 |
| D | ARG177 |
| D | ILE181 |
| D | GLY182 |
| D | TRP186 |
| D | ASN220 |
| D | SER224 |
| D | ARG227 |
| D | GLU228 |
| D | LEU281 |
| D | TRP288 |
| D | ARG294 |
| D | TYR295 |
| D | MG402 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 402 |
| Chain | Residue |
| D | ASN220 |
| D | SER224 |
| D | GLU228 |
| D | GGS401 |
| D | HOH527 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Motif: {"description":"DDXXD motif; degenerate"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Motif: {"description":"NSE/DTE motif"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q40577","evidenceCode":"ECO:0000250"}]} |
