Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008716 | molecular_function | D-alanine-D-alanine ligase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP A 310 |
| Chain | Residue |
| A | LYS97 |
| A | LYS181 |
| A | TRP182 |
| A | LEU183 |
| A | GLU187 |
| A | PHE209 |
| A | TYR210 |
| A | LYS215 |
| A | ASP257 |
| A | MET259 |
| A | LEU269 |
| A | ILE142 |
| A | GLU270 |
| A | DS0311 |
| A | MG330 |
| A | MG331 |
| A | HOH2135 |
| A | HOH2137 |
| A | HOH2238 |
| A | LYS144 |
| A | GLU148 |
| A | GLY149 |
| A | SER150 |
| A | SER151 |
| A | MET154 |
| A | GLU180 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DS0 A 311 |
| 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 | ADP310 |
| A | MG330 |
| A | MG331 |
| A | HOH2028 |
| A | HOH2080 |
| A | HOH2190 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 330 |
| Chain | Residue |
| A | GLU270 |
| A | ASN272 |
| A | ADP310 |
| A | DS0311 |
| A | MG331 |
| A | HOH2135 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 331 |
| Chain | Residue |
| A | ASP257 |
| A | GLU270 |
| A | ADP310 |
| A | DS0311 |
| A | MG330 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ADP B 310 |
| Chain | Residue |
| B | LYS97 |
| B | ILE142 |
| B | LYS144 |
| B | GLU148 |
| B | GLY149 |
| B | SER150 |
| B | SER151 |
| B | MET154 |
| B | GLU180 |
| B | LYS181 |
| B | TRP182 |
| B | LEU183 |
| B | GLU187 |
| B | PHE209 |
| B | TYR210 |
| B | LYS215 |
| B | ASP257 |
| B | MET259 |
| B | GLU270 |
| B | DS0311 |
| B | MG330 |
| B | MG331 |
| B | HOH2059 |
| B | HOH2077 |
| B | HOH2101 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE DS0 B 311 |
| Chain | Residue |
| B | GLU15 |
| B | HIS63 |
| B | GLY149 |
| B | SER150 |
| B | LYS215 |
| B | TYR216 |
| B | ARG255 |
| B | ASP257 |
| B | GLU270 |
| B | ASN272 |
| B | PRO275 |
| B | GLY276 |
| B | ADP310 |
| B | MG330 |
| B | MG331 |
| B | HOH2006 |
| B | HOH2020 |
| B | HOH2077 |
| B | HOH2078 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 330 |
| Chain | Residue |
| B | ASN272 |
| B | ADP310 |
| B | DS0311 |
| B | MG331 |
| B | GLU270 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 331 |
| Chain | Residue |
| B | ASP257 |
| B | GLU270 |
| B | ADP310 |
| B | DS0311 |
| B | MG330 |
| B | HOH2077 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1307 |
| Chain | Residue |
| A | GLU17 |
| A | VAL18 |
| A | TYR212 |
| A | LEU217 |
| A | ARG288 |
| A | HOH2034 |
| A | HOH2035 |
| A | HOH2239 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1308 |
| Chain | Residue |
| A | ASP41 |
| A | GLU44 |
| A | ASN161 |
| A | GLN164 |
| A | ASP165 |
| A | ARG168 |
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 | 404 |
| Details | Domain: {"description":"ATP-grasp"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 116 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 883 |
| Chain | Residue | Details |
| A | GLU15 | electrostatic stabiliser, steric locator |
| A | SER150 | electrostatic stabiliser |
| A | TYR216 | activator |
| A | ARG255 | electrostatic stabiliser, steric locator |
| A | ASP257 | metal ligand |
| A | GLU270 | metal ligand |
| A | ASN272 | metal ligand |
| A | GLY276 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 883 |
| Chain | Residue | Details |
| B | GLU15 | electrostatic stabiliser, steric locator |
| B | SER150 | electrostatic stabiliser |
| B | TYR216 | activator |
| B | ARG255 | electrostatic stabiliser, steric locator |
| B | ASP257 | metal ligand |
| B | GLU270 | metal ligand |
| B | ASN272 | metal ligand |
| B | GLY276 | electrostatic stabiliser |
