Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine 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 | 0051301 | biological_process | cell division |
A | 0071555 | biological_process | cell wall organization |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008360 | biological_process | regulation of cell shape |
B | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine ligase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0016881 | molecular_function | acid-amino acid ligase activity |
B | 0051301 | biological_process | cell division |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 776 |
Chain | Residue |
A | HIS198 |
A | EPU598 |
A | HOH1014 |
A | HOH1089 |
A | HOH1090 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 710 |
Chain | Residue |
B | HOH1152 |
B | HOH1148 |
B | HOH1149 |
B | HOH1150 |
B | HOH1151 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | HIS198 |
B | EPU602 |
B | HOH732 |
B | HOH735 |
B | HOH736 |
B | HOH737 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 611 |
Chain | Residue |
A | HOH962 |
A | HOH1058 |
A | HOH1059 |
A | HOH1060 |
A | HOH1061 |
site_id | AC5 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE EPU A 598 |
Chain | Residue |
A | GLY25 |
A | GLY27 |
A | GLY28 |
A | ALA29 |
A | GLY30 |
A | MSE31 |
A | ASP49 |
A | ILE50 |
A | HIS70 |
A | SER84 |
A | SER85 |
A | ILE87 |
A | ARG107 |
A | GLU173 |
A | ASP175 |
A | SER177 |
A | HIS198 |
A | MG776 |
A | HOH812 |
A | HOH905 |
A | HOH914 |
A | HOH935 |
A | HOH986 |
A | HOH987 |
A | HOH988 |
A | HOH992 |
A | HOH999 |
A | HOH1014 |
A | HOH1090 |
site_id | AC6 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE EPU B 602 |
Chain | Residue |
B | GLY25 |
B | GLY27 |
B | GLY28 |
B | ALA29 |
B | GLY30 |
B | MSE31 |
B | ASP49 |
B | ILE50 |
B | HIS70 |
B | SER84 |
B | SER85 |
B | ALA86 |
B | ILE87 |
B | ARG107 |
B | GLU173 |
B | ASP175 |
B | SER177 |
B | HIS198 |
B | MG601 |
B | HOH614 |
B | HOH619 |
B | HOH626 |
B | HOH653 |
B | HOH654 |
B | HOH735 |
B | HOH737 |
B | HOH746 |
B | HOH863 |
B | HOH915 |
B | HOH955 |
B | HOH956 |
B | HOH1071 |
B | HOH1158 |
B | HOH1160 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY125 | |
B | GLY125 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1p3d |
Chain | Residue | Details |
A | LYS129 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1p3d |
Chain | Residue | Details |
B | LYS129 | |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 876 |
Chain | Residue | Details |
A | LYS129 | electrostatic stabiliser |
A | THR130 | metal ligand |
A | GLU173 | metal ligand |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 876 |
Chain | Residue | Details |
B | LYS129 | electrostatic stabiliser |
B | THR130 | metal ligand |
B | GLU173 | metal ligand |