4D9K
Crystal structure of Escherichia coli Diaminopropionate ammonia lyase in apo form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008838 | molecular_function | diaminopropionate ammonia-lyase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0008838 | molecular_function | diaminopropionate ammonia-lyase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0008838 | molecular_function | diaminopropionate ammonia-lyase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0008838 | molecular_function | diaminopropionate ammonia-lyase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 501 |
| Chain | Residue |
| A | LYS77 |
| A | ALA231 |
| A | GLY232 |
| A | VAL233 |
| A | GLY234 |
| A | ALA235 |
| A | MET236 |
| A | HOH637 |
| A | HOH640 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 502 |
| Chain | Residue |
| A | ARG218 |
| A | THR223 |
| A | TYR248 |
| A | HOH631 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 503 |
| Chain | Residue |
| A | GLN357 |
| A | HOH646 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 D 401 |
| Chain | Residue |
| D | LYS77 |
| D | TYR206 |
| D | ALA231 |
| D | VAL233 |
| D | GLY234 |
| D | ALA235 |
| D | MET236 |
| D | HOH524 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 401 |
| Chain | Residue |
| B | PHE76 |
| B | LYS77 |
| B | ALA231 |
| B | GLY232 |
| B | VAL233 |
| B | GLY234 |
| B | ALA235 |
| B | MET236 |
| B | HOH554 |
| B | HOH617 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 401 |
| Chain | Residue |
| C | ALA231 |
| C | GLY232 |
| C | VAL233 |
| C | GLY234 |
| C | ALA235 |
| C | MET236 |
| C | HOH550 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 402 |
| Chain | Residue |
| C | ARG218 |
| C | THR223 |
| C | TYR248 |
| C | HOH530 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; for D-DAP ammonia-lyase activity => ECO:0000305 |
| Chain | Residue | Details |
| A | LYS77 | |
| D | LYS77 | |
| B | LYS77 | |
| C | LYS77 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; for L-DAP ammonia-lyase activity => ECO:0000305 |
| Chain | Residue | Details |
| A | ASP120 | |
| D | ASP120 | |
| B | ASP120 | |
| C | ASP120 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS77 | |
| D | LYS77 | |
| B | LYS77 | |
| C | LYS77 |
