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 | 20 |
Details | BINDING SITE FOR RESIDUE D17 A 1441 |
Chain | Residue |
A | ILE11 |
A | ALA414 |
A | SER415 |
A | LEU416 |
A | ASN421 |
A | PHE422 |
A | SO41451 |
A | HOH2525 |
A | HOH2526 |
A | HOH2528 |
A | HOH2529 |
A | ASP35 |
A | HOH2530 |
A | THR36 |
A | ARG37 |
A | SER71 |
A | PRO72 |
A | PHE161 |
A | HIS183 |
A | LYS348 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 1442 |
Chain | Residue |
A | GLY73 |
A | ARG186 |
A | LEU416 |
A | HOH2265 |
A | HOH2529 |
A | HOH2531 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE AZI A 1443 |
Chain | Residue |
A | ASP417 |
A | GLN418 |
A | PHE419 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE AZI A 1444 |
Chain | Residue |
A | ALA329 |
A | ASN331 |
A | LEU333 |
A | HOH2532 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE AZI A 1445 |
Chain | Residue |
A | PRO300 |
A | ARG302 |
A | PHE422 |
A | GLU423 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE AZI A 1446 |
Chain | Residue |
A | LEU339 |
A | ASN363 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE AZI A 1447 |
Chain | Residue |
A | ALA102 |
A | ALA104 |
A | PRO105 |
A | HOH2164 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 1448 |
Chain | Residue |
A | ASN113 |
A | GLY114 |
A | LYS115 |
A | SER116 |
A | THR117 |
A | ARG302 |
A | HOH2533 |
A | HOH2534 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1449 |
Chain | Residue |
A | THR166 |
A | SER167 |
A | SER168 |
A | LEU169 |
A | ARG200 |
A | GLU203 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1450 |
Chain | Residue |
A | HIS309 |
A | ASN310 |
A | SER438 |
A | HIS439 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 1451 |
Chain | Residue |
A | GLY14 |
A | LEU15 |
A | THR16 |
A | D171441 |
A | HOH2024 |
A | HOH2526 |
A | HOH2535 |
A | HOH2536 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1452 |
Chain | Residue |
A | ARG37 |
A | MET38 |
A | GLN170 |
A | HOH2537 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 1453 |
Chain | Residue |
A | HIS309 |
A | ASN310 |
A | HOH2055 |
A | HOH2057 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL A 1454 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 1455 |
Chain | Residue |
A | TYR3 |
A | GLN4 |
A | ARG27 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 1456 |
Chain | Residue |
A | GLU96 |
A | THR165 |
A | SER167 |
A | HOH2149 |
site_id | BC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 1457 |
Chain | Residue |
A | LEU57 |
A | HOH2127 |
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 |