Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008764 | molecular_function | UDP-N-acetylmuramoylalanine-D-glutamate 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 | 0042802 | molecular_function | identical protein binding |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 1000 |
| Chain | Residue |
| A | ASP182 |
| A | HIS183 |
| A | UMA450 |
| A | HOH1096 |
| A | HOH1173 |
| A | HOH1177 |
| A | HOH1255 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1001 |
| Chain | Residue |
| A | SER116 |
| A | GLU157 |
| A | ADP451 |
| A | HOH1126 |
| A | HOH1309 |
| A | HOH1310 |
| site_id | AC3 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE UMA A 450 |
| Chain | Residue |
| A | LEU15 |
| A | THR16 |
| A | ASP35 |
| A | THR36 |
| A | ARG37 |
| A | SER71 |
| A | PRO72 |
| A | GLY73 |
| A | GLY137 |
| A | ASN138 |
| A | GLY140 |
| A | PHE161 |
| A | GLN162 |
| A | HIS183 |
| A | PHE422 |
| A | MG1000 |
| A | HOH1003 |
| A | HOH1004 |
| A | HOH1056 |
| A | HOH1066 |
| A | HOH1094 |
| A | HOH1096 |
| A | HOH1155 |
| A | HOH1173 |
| A | HOH1233 |
| A | HOH1255 |
| A | HOH1261 |
| A | HOH1270 |
| A | HOH1292 |
| A | HOH1309 |
| A | HOH1319 |
| A | HOH1341 |
| A | HOH1368 |
| A | HOH1370 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP A 451 |
| Chain | Residue |
| A | ASN113 |
| A | GLY114 |
| A | LYS115 |
| A | SER116 |
| A | THR117 |
| A | GLU157 |
| A | ASN178 |
| A | HIS267 |
| A | ASN271 |
| A | ARG302 |
| A | ASP317 |
| A | LYS319 |
| A | ALA320 |
| A | SER325 |
| A | ALA328 |
| A | MG1001 |
| A | HOH1010 |
| A | HOH1097 |
| A | HOH1232 |
| A | HOH1241 |
| A | HOH1309 |
| A | HOH1310 |
| A | HOH1313 |
| site_id | MG1 |
| Number of Residues | 6 |
| Details | MAGNESIUM SITE 1: OCTAHEDRAL COORDINATION LIGANDS: ONE OF THE CARBOXYL OXYGENS OF UMA, NE2 OF HIS 183 AND FOUR WATERS. |
| Chain | Residue |
| A | HIS183 |
| A | UMA450 |
| A | HOH1096 |
| A | HOH1173 |
| A | HOH1177 |
| A | HOH1255 |
| site_id | MG2 |
| Number of Residues | 6 |
| Details | MAGNESIUM SITE 2: OCTAHEDRAL COORDINATION LIGANDS: ONE OF THE BETA-PHOSPHORYL OXYGENS OF ADP, OG OF SER 116, OE2 OF GLU 157 AND THREE WATERS. |
| Chain | Residue |
| A | HOH1126 |
| A | HOH1309 |
| A | HOH1310 |
| A | SER116 |
| A | GLU157 |
| A | ADP451 |
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. GSNGKSTVTTLVGEMA |
| Chain | Residue | Details |
| A | GLY111-ALA126 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1p3d |
| Chain | Residue | Details |
| A | LYS115 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1p3d |
| Chain | Residue | Details |
| A | ASN138 | |
| A | HIS183 | |
| A | LYS115 | |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 317 |
| Chain | Residue | Details |
| A | LYS115 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
| A | ASN138 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | HIS183 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |
