Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 461 |
| Chain | Residue |
| A | ASN113 |
| A | GLY114 |
| A | LYS115 |
| A | SER116 |
| A | THR117 |
| A | ARG302 |
| A | LYS319 |
| A | HOH643 |
| A | HOH646 |
| site_id | AC2 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE UAG A 460 |
| Chain | Residue |
| A | GLY14 |
| A | LEU15 |
| A | THR16 |
| A | ASP35 |
| A | THR36 |
| A | ARG37 |
| A | SER71 |
| A | PRO72 |
| A | GLY73 |
| A | GLY137 |
| A | ASN138 |
| A | GLY140 |
| A | SER159 |
| A | PHE161 |
| A | GLN162 |
| A | HIS183 |
| A | THR321 |
| A | LYS348 |
| A | ALA414 |
| A | SER415 |
| A | ASN421 |
| A | PHE422 |
| A | HOH501 |
| A | HOH502 |
| A | HOH529 |
| A | HOH554 |
| A | HOH565 |
| A | HOH594 |
| A | HOH600 |
| A | HOH684 |
| A | HOH906 |
| A | HOH912 |
| A | HOH956 |
| A | HOH958 |
| A | UNX986 |
| A | UNX990 |
| A | UNX991 |
| A | UNX992 |
| A | UNX993 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UNX A 986 |
| Chain | Residue |
| A | ASN138 |
| A | ILE139 |
| A | UAG460 |
| A | HOH624 |
| A | HOH904 |
| A | UNX987 |
| A | UNX990 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE UNX A 987 |
| Chain | Residue |
| A | SER116 |
| A | ASN138 |
| A | GLU157 |
| A | LYS319 |
| A | UNX986 |
| A | UNX988 |
| A | UNX989 |
| A | UNX990 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE UNX A 988 |
| Chain | Residue |
| A | LYS319 |
| A | HOH942 |
| A | UNX987 |
| A | UNX989 |
| A | UNX990 |
| A | UNX991 |
| A | UNX992 |
| A | UNX993 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UNX A 989 |
| Chain | Residue |
| A | ASN138 |
| A | UNX987 |
| A | UNX988 |
| A | UNX990 |
| A | UNX991 |
| A | UNX992 |
| A | UNX993 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE UNX A 990 |
| Chain | Residue |
| A | ASN138 |
| A | UAG460 |
| A | UNX986 |
| A | UNX987 |
| A | UNX988 |
| A | UNX989 |
| A | UNX991 |
| A | UNX992 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UNX A 991 |
| Chain | Residue |
| A | PHE422 |
| A | UAG460 |
| A | UNX988 |
| A | UNX989 |
| A | UNX990 |
| A | UNX992 |
| A | UNX993 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE UNX A 992 |
| Chain | Residue |
| A | UNX991 |
| A | UNX993 |
| A | ASN138 |
| A | UAG460 |
| A | HOH920 |
| A | UNX988 |
| A | UNX989 |
| A | UNX990 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE UNX A 993 |
| Chain | Residue |
| A | THR321 |
| A | UAG460 |
| A | HOH920 |
| A | HOH942 |
| A | UNX988 |
| A | UNX989 |
| A | UNX991 |
| A | UNX992 |
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 | 1 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY111 | |
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 |
