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 T26 A 500 |
Chain | Residue |
A | ILE11 |
A | ALA414 |
A | SER415 |
A | ASN421 |
A | PHE422 |
A | DMS600 |
A | DMS603 |
A | SO41444 |
A | HOH2402 |
A | HOH2403 |
A | HOH2404 |
A | ASP35 |
A | HOH2405 |
A | HOH2406 |
A | HOH2407 |
A | HOH2408 |
A | HOH2409 |
A | THR36 |
A | ARG37 |
A | SER71 |
A | ILE139 |
A | PHE161 |
A | HIS183 |
A | LYS319 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 600 |
Chain | Residue |
A | GLY73 |
A | ARG186 |
A | LEU416 |
A | T26500 |
A | HOH2409 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS A 601 |
Chain | Residue |
A | LEU163 |
A | THR166 |
A | SER167 |
A | SER168 |
A | LEU169 |
A | ARG200 |
A | GLU203 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 603 |
Chain | Residue |
A | PRO72 |
A | SER159 |
A | GLN162 |
A | T26500 |
A | HOH2180 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 604 |
Chain | Residue |
A | ASN7 |
A | ALA64 |
A | HIS309 |
A | ASN310 |
A | HOH2094 |
A | HOH2410 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 1441 |
Chain | Residue |
A | ASN113 |
A | GLY114 |
A | LYS115 |
A | SER116 |
A | THR117 |
A | ARG302 |
A | LYS319 |
A | HOH2411 |
A | HOH2412 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1442 |
Chain | Residue |
A | HIS309 |
A | ASN310 |
A | SER438 |
A | HIS439 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1444 |
Chain | Residue |
A | GLY14 |
A | LEU15 |
A | THR16 |
A | ILE139 |
A | T26500 |
A | HOH2413 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1445 |
Chain | Residue |
A | ARG37 |
A | MET38 |
A | GLN170 |
A | HOH2415 |
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 |