Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008765 | molecular_function | UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016881 | molecular_function | acid-amino acid ligase activity |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008765 | molecular_function | UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016881 | molecular_function | acid-amino acid ligase activity |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue IPA A 1101 |
| Chain | Residue |
| A | ARG110 |
| A | LEU322 |
| A | GLY323 |
| B | ASP107 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SZK A 1102 |
| Chain | Residue |
| A | LYS225 |
| A | LEU228 |
| A | TYR229 |
| A | ILE239 |
| A | TRP249 |
| A | THR115 |
| A | LEU189 |
| A | SER202 |
| A | VAL203 |
| A | PHE204 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue IPA B 701 |
| Chain | Residue |
| B | GLY119 |
| B | LYS120 |
| B | THR121 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue IPA B 702 |
| Chain | Residue |
| B | MET261 |
| B | ALA276 |
| B | THR277 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue SZK B 703 |
| Chain | Residue |
| B | THR115 |
| B | LEU189 |
| B | SER202 |
| B | VAL203 |
| B | PHE204 |
| B | LYS225 |
| B | LEU228 |
| B | TYR229 |
| B | HIS232 |
| B | ALA237 |
| B | ILE239 |
| B | TRP249 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU27 | |
| A | ASP414 | |
| A | GLY465 | |
| A | GLU469 | |
| B | LEU27 | |
| B | SER29 | |
| B | HIS44 | |
| B | ASN157 | |
| B | THR158 | |
| B | SER185 | |
| B | GLN191 | |
| A | SER29 | |
| B | ARG193 | |
| B | ARG390 | |
| B | ASP414 | |
| B | GLY465 | |
| B | GLU469 | |
| A | HIS44 | |
| A | ASN157 | |
| A | THR158 | |
| A | SER185 | |
| A | GLN191 | |
| A | ARG193 | |
| A | ARG390 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY116 | |
| B | GLY116 | |
| Chain | Residue | Details |
| A | LYS225 | |
| B | LYS225 | |
