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 | 24 |
Details | BINDING SITE FOR RESIDUE UMA A 450 |
Chain | Residue |
A | GLY14 |
A | GLY137 |
A | ASN138 |
A | GLY140 |
A | SER159 |
A | GLN162 |
A | HIS183 |
A | HOH2009 |
A | HOH2010 |
A | HOH2012 |
A | HOH2059 |
A | LEU15 |
A | HOH2071 |
A | HOH2095 |
A | HOH2265 |
A | HOH2266 |
A | HOH2267 |
A | THR16 |
A | ASP35 |
A | THR36 |
A | ARG37 |
A | SER71 |
A | PRO72 |
A | GLY73 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE ADP A 451 |
Chain | Residue |
A | ASN113 |
A | GLY114 |
A | LYS115 |
A | SER116 |
A | THR117 |
A | ASN178 |
A | HIS267 |
A | ASN271 |
A | ARG302 |
A | PHE303 |
A | ASP317 |
A | LYS319 |
A | ALA320 |
A | SER325 |
A | ALA328 |
A | HOH2068 |
A | HOH2071 |
A | HOH2072 |
A | HOH2074 |
A | HOH2119 |
A | HOH2184 |
A | HOH2268 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MLI A 500 |
Chain | Residue |
A | THR321 |
A | ALA414 |
A | SER415 |
A | ASN421 |
A | PHE422 |
A | HOH2212 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MLI A 501 |
Chain | Residue |
A | HIS241 |
A | THR246 |
A | HIS334 |
A | HOH2181 |
A | HOH2269 |
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 | 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 |