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 | 0007049 | biological_process | cell cycle |
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 | 22 |
Details | BINDING SITE FOR RESIDUE T04 A 500 |
Chain | Residue |
A | ILE11 |
A | ALA414 |
A | SER415 |
A | ASN421 |
A | PHE422 |
A | SO41442 |
A | HOH2166 |
A | HOH2193 |
A | HOH2234 |
A | HOH2439 |
A | HOH2440 |
A | ASP35 |
A | HOH2441 |
A | HOH2443 |
A | HOH2447 |
A | THR36 |
A | ARG37 |
A | SER71 |
A | ASN138 |
A | PHE161 |
A | HIS183 |
A | LYS348 |
site_id | AC2 |
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 | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 604 |
Chain | Residue |
A | ASN7 |
A | ARG32 |
A | ALA64 |
A | GLU308 |
A | HIS309 |
A | ASN310 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE AZI A 700 |
Chain | Residue |
A | GLN418 |
A | PHE419 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE AZI A 701 |
Chain | Residue |
A | ALA329 |
A | ASN331 |
A | GLY332 |
A | LEU333 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE AZI A 703 |
Chain | Residue |
A | LEU339 |
A | ASN363 |
A | VAL364 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE AZI A 704 |
Chain | Residue |
A | ALA104 |
A | PRO105 |
A | HOH2138 |
A | HOH2444 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 1440 |
Chain | Residue |
A | ASN113 |
A | GLY114 |
A | LYS115 |
A | SER116 |
A | THR117 |
A | ARG302 |
A | HOH2445 |
A | HOH2446 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1441 |
Chain | Residue |
A | HIS309 |
A | ASN310 |
A | SER438 |
A | HIS439 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 1442 |
Chain | Residue |
A | GLY14 |
A | LEU15 |
A | THR16 |
A | T04500 |
A | HOH2447 |
A | HOH2448 |
A | HOH2449 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1443 |
Chain | Residue |
A | ARG37 |
A | MET38 |
A | GLN170 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1444 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 1445 |
Chain | Residue |
A | SER56 |
A | LEU57 |
A | HOH2103 |
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 |