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 | 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 | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 800 |
Chain | Residue |
A | LYS115 |
A | SER159 |
A | SER160 |
A | TYR194 |
A | LYS198 |
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 | 6 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
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 | 2 |
Details | Annotated By Reference To The Literature 1p3d |
Chain | Residue | Details |
A | ASN138 | |
A | LYS115 | |
site_id | MCSA1 |
Number of Residues | 2 |
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 |