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 | 7 |
Details | BINDING SITE FOR RESIDUE MN A 1000 |
Chain | Residue |
A | HOH716 |
A | HOH837 |
A | ASP182 |
A | HIS183 |
A | UMA450 |
A | HOH600 |
A | HOH712 |
site_id | AC2 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE UMA A 450 |
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 | PHE161 |
A | GLN162 |
A | HIS183 |
A | LYS319 |
A | HOH501 |
A | HOH502 |
A | HOH529 |
A | HOH554 |
A | HOH565 |
A | HOH598 |
A | HOH600 |
A | HOH682 |
A | HOH684 |
A | HOH809 |
A | HOH837 |
A | HOH844 |
A | HOH864 |
A | MN1000 |
site_id | AC3 |
Number of Residues | 19 |
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 | HOH508 |
A | HOH601 |
A | HOH805 |
A | HOH819 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE EPE A 452 |
Chain | Residue |
A | MET38 |
A | THR39 |
A | LEU43 |
A | ARG52 |
A | THR54 |
A | CYS99 |
A | ALA102 |
A | ALA104 |
A | PRO105 |
A | ILE106 |
A | SER168 |
A | LEU169 |
A | GLN170 |
site_id | MN1 |
Number of Residues | 4 |
Details | MANGANESE SITE 1: OCTAHEDRAL COORDINATION LIGANDS: ONE OF THE CARBOXYL OXYGENS OF UMA, NE2 OF HIS 183 AND FOUR WATERS. |
Chain | Residue |
A | HOH600 |
A | HOH712 |
A | HOH716 |
A | HOH837 |
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 | SER112 | |
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 | SER116 | activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity |
A | ILE139 | electrostatic stabiliser, hydrogen bond donor, steric role |
A | MET184 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role |