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 | 21 |
| Details | BINDING SITE FOR RESIDUE LK4 A1440 |
| Chain | Residue |
| A | ILE11 |
| A | HIS183 |
| A | LYS348 |
| A | ALA414 |
| A | SER415 |
| A | LEU416 |
| A | ASN421 |
| A | PHE422 |
| A | HOH2187 |
| A | HOH2412 |
| A | HOH2413 |
| A | GLY12 |
| A | HOH2414 |
| A | HOH2415 |
| A | ASP35 |
| A | THR36 |
| A | ARG37 |
| A | LEU57 |
| A | SER71 |
| A | GLY73 |
| A | PHE161 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A1441 |
| Chain | Residue |
| A | ASN113 |
| A | GLY114 |
| A | LYS115 |
| A | SER116 |
| A | THR117 |
| A | ARG302 |
| A | LYS319 |
| A | HOH2416 |
| A | HOH2417 |
| A | HOH2418 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A1442 |
| Chain | Residue |
| A | THR166 |
| A | SER167 |
| A | SER168 |
| A | LEU169 |
| A | ARG200 |
| A | GLU203 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A1443 |
| Chain | Residue |
| A | HIS309 |
| A | ASN310 |
| A | SER438 |
| A | HIS439 |
| A | HIS440 |
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 |
