Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008716 | molecular_function | D-alanine-D-alanine ligase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 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 330 |
| Chain | Residue |
| A | LYS215 |
| A | ASP257 |
| A | GLU270 |
| A | ADP310 |
| A | PHY320 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 331 |
| Chain | Residue |
| A | GLU270 |
| A | ASN272 |
| A | ADP310 |
| A | PHY320 |
| A | HOH400 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP A 310 |
| Chain | Residue |
| A | LYS97 |
| A | ILE142 |
| A | LYS144 |
| A | GLU148 |
| A | GLY149 |
| A | SER150 |
| A | SER151 |
| A | MET154 |
| A | GLU180 |
| A | LYS181 |
| A | TRP182 |
| A | LEU183 |
| A | GLU187 |
| A | TYR210 |
| A | LYS215 |
| A | ASP257 |
| A | LEU269 |
| A | GLU270 |
| A | PHY320 |
| A | MG330 |
| A | MG331 |
| A | HOH413 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE PHY A 320 |
| Chain | Residue |
| A | GLU15 |
| A | GLY149 |
| A | SER150 |
| A | LYS215 |
| A | TYR216 |
| A | ARG255 |
| A | ASP257 |
| A | GLU270 |
| A | ASN272 |
| A | PRO275 |
| A | GLY276 |
| A | SER281 |
| A | LEU282 |
| A | ADP310 |
| A | MG330 |
| A | MG331 |
| A | HOH400 |
| A | HOH430 |
| A | HOH531 |
| A | HOH637 |
| A | HOH654 |
| site_id | ADP |
| Number of Residues | 15 |
| Details | |
| Chain | Residue |
| A | LYS97 |
| A | LYS215 |
| A | MET259 |
| A | GLU270 |
| A | ASN272 |
| A | MG330 |
| A | MG331 |
| A | ILE142 |
| A | LYS144 |
| A | SER150 |
| A | SER151 |
| A | GLU180 |
| A | TRP182 |
| A | GLU187 |
| A | PHE209 |
| site_id | PHY |
| Number of Residues | 6 |
| Details | |
| Chain | Residue |
| A | GLU15 |
| A | VAL18 |
| A | HIS63 |
| A | SER150 |
| A | TYR216 |
| A | SER281 |
Functional Information from PROSITE/UniProt
| site_id | PS00843 |
| Number of Residues | 12 |
| Details | DALA_DALA_LIGASE_1 D-alanine--D-alanine ligase signature 1. HGrgGEDGtLQG |
| Chain | Residue | Details |
| A | HIS63-GLY74 | |
| site_id | PS00844 |
| Number of Residues | 29 |
| Details | DALA_DALA_LIGASE_2 D-alanine--D-alanine ligase signature 2. LgckGwGRIDVMldsdgqfy....LlEANTsPG |
| Chain | Residue | Details |
| A | LEU248-GLY276 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | ARG16 | |
| A | SER151 | |
| A | LEU282 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER135 | |
| A | VAL258 | |
| A | ALA271 | |
| A | THR273 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | |
| Chain | Residue | Details |
| A | GLU15 | |
| A | TYR216 | |
| A | GLY276 | |
| A | ARG255 | |
| A | SER150 | |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 883 |
| Chain | Residue | Details |
| A | ARG16 | electrostatic stabiliser, steric locator |
| A | SER151 | electrostatic stabiliser |
| A | LEU217 | activator |
| A | ILE256 | electrostatic stabiliser, steric locator |
| A | VAL258 | metal ligand |
| A | ALA271 | metal ligand |
| A | THR273 | metal ligand |
| A | MET277 | electrostatic stabiliser |
