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 |
B | 0003824 | molecular_function | catalytic activity |
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 | 6 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | SER281 | |
B | GLU15 | |
B | SER150 | |
B | SER281 | |
A | GLU15 | |
A | SER150 | |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | GLU270 | |
B | ASN272 | |
A | ILE134 | |
A | ASP257 | |
A | GLU270 | |
A | ASN272 | |
B | ILE134 | |
B | ASP257 | |
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 |