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 | 4 |
Details | BINDING SITE FOR RESIDUE MG A 330 |
Chain | Residue |
A | ASP257 |
A | GLU270 |
A | ADP310 |
A | POB321 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 331 |
Chain | Residue |
A | GLY149 |
A | GLU270 |
A | ASN272 |
A | ADP310 |
A | POB321 |
A | HOH536 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 332 |
Chain | Residue |
A | SER94 |
A | GLU270 |
A | ALA271 |
A | HOH522 |
site_id | AC4 |
Number of Residues | 23 |
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 | MET259 |
A | LEU269 |
A | GLU270 |
A | POB321 |
A | MG330 |
A | MG331 |
A | HOH511 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE POB A 321 |
Chain | Residue |
A | GLU15 |
A | GLY149 |
A | SER150 |
A | TYR210 |
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 | HOH508 |
A | HOH536 |
A | HOH538 |
site_id | ADP |
Number of Residues | 12 |
Details | ADP BINDING SITE. |
Chain | Residue |
A | LYS97 |
A | ALA159 |
A | ILE142 |
A | PHE209 |
A | LYS144 |
A | LYS215 |
A | GLU270 |
A | ASN272 |
A | SER151 |
A | GLU180 |
A | GLU187 |
A | TRP182 |
site_id | LIG |
Number of Residues | 6 |
Details | LIGAND BINDING SITE. |
Chain | Residue |
A | GLU15 |
A | SER150 |
A | TYR216 |
A | VAL18 |
A | HIS63 |
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 | Annotated By Reference To The Literature 2dln |
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 |