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 | 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 | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0008716 | molecular_function | D-alanine-D-alanine ligase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071555 | biological_process | cell wall organization |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0008716 | molecular_function | D-alanine-D-alanine ligase activity |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP A 370 |
| Chain | Residue |
| A | LYS141 |
| A | ILE224 |
| A | GLU228 |
| A | LEU249 |
| A | PHE304 |
| A | ASN314 |
| A | GLU315 |
| A | MG372 |
| A | HOH494 |
| A | PHE183 |
| A | LYS185 |
| A | GLY190 |
| A | SER191 |
| A | SER192 |
| A | GLU221 |
| A | GLN222 |
| A | GLY223 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 371 |
| Chain | Residue |
| A | PRO126 |
| A | PHE127 |
| A | ALA350 |
| A | ARG353 |
| A | HIS354 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 372 |
| Chain | Residue |
| A | GLU315 |
| A | ADP370 |
| A | HOH493 |
| A | HOH494 |
| A | HOH495 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 373 |
| Chain | Residue |
| A | ASN236 |
| A | ASP237 |
| A | CYS295 |
| A | ALA296 |
| A | ARG353 |
| A | HOH375 |
| A | HOH383 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP B 370 |
| Chain | Residue |
| B | LYS141 |
| B | PHE183 |
| B | LYS185 |
| B | GLY190 |
| B | SER191 |
| B | SER192 |
| B | GLU221 |
| B | GLN222 |
| B | GLY223 |
| B | ILE224 |
| B | GLU228 |
| B | PHE304 |
| B | ASN314 |
| B | GLU315 |
| B | MG371 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 371 |
| Chain | Residue |
| B | ASP302 |
| B | GLU315 |
| B | ADP370 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 372 |
| Chain | Residue |
| B | GLN240 |
| B | ARG345 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 373 |
| Chain | Residue |
| B | HIS85 |
| B | GLN86 |
| B | LEU87 |
| B | LEU96 |
| B | PRO97 |
| B | THR98 |
| B | VAL99 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 374 |
| Chain | Residue |
| B | ASN236 |
| B | CYS295 |
| B | ALA296 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 375 |
| Chain | Residue |
| B | ARG300 |
| B | GLY321 |
| B | SER326 |
| B | MSE327 |
| B | HOH365 |
| B | HOH415 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 376 |
| Chain | Residue |
| B | CYS138 |
| B | MSE139 |
| B | LYS141 |
| B | ALA187 |
| B | GLN189 |
| B | GLU315 |
| B | ILE316 |
| B | ASN317 |
| B | HOH386 |
| site_id | BC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP C 370 |
| Chain | Residue |
| C | PHE183 |
| C | LYS185 |
| C | GLY190 |
| C | SER191 |
| C | SER192 |
| C | GLU221 |
| C | GLN222 |
| C | GLY223 |
| C | ILE224 |
| C | GLU228 |
| C | PHE304 |
| C | ASN314 |
| C | GLU315 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C 371 |
| Chain | Residue |
| C | ARG300 |
| C | GLY321 |
| C | SER326 |
| C | MSE327 |
| C | HOH416 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 372 |
| Chain | Residue |
| C | ALA350 |
| C | ARG353 |
| C | HIS354 |
| C | HOH397 |
| C | PRO126 |
| C | PHE127 |
| site_id | BC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP D 370 |
| Chain | Residue |
| D | LYS141 |
| D | PHE183 |
| D | LYS185 |
| D | GLN189 |
| D | GLY190 |
| D | SER191 |
| D | SER192 |
| D | GLU221 |
| D | GLN222 |
| D | GLY223 |
| D | ILE224 |
| D | GLU228 |
| D | LEU249 |
| D | PHE304 |
| D | ASN314 |
| D | GLU315 |
| D | MG372 |
| D | HOH470 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT D 371 |
| Chain | Residue |
| D | PRO126 |
| D | PHE127 |
| D | ALA350 |
| D | ARG353 |
| D | HIS354 |
| D | HOH469 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 372 |
| Chain | Residue |
| D | GLU315 |
| D | ADP370 |
| D | HOH470 |
| D | HOH471 |
| D | HOH472 |
Functional Information from PROSITE/UniProt
| site_id | PS00843 |
| Number of Residues | 12 |
| Details | DALA_DALA_LIGASE_1 D-alanine--D-alanine ligase signature 1. HGtlGEDGsLQG |
| Chain | Residue | Details |
| A | HIS107-GLY118 | |
| site_id | PS00844 |
| Number of Residues | 29 |
| Details | DALA_DALA_LIGASE_2 D-alanine--D-alanine ligase signature 2. LgcaGmARVDVFltadnevv....InEINTlPG |
| Chain | Residue | Details |
| A | LEU293-GLY321 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU175 | |
| C | ASP302 | |
| C | GLU315 | |
| C | ASN317 | |
| D | GLU175 | |
| D | ASP302 | |
| D | GLU315 | |
| D | ASN317 | |
| A | ASP302 | |
| A | GLU315 | |
| A | ASN317 | |
| B | GLU175 | |
| B | ASP302 | |
| B | GLU315 | |
| B | ASN317 | |
| C | GLU175 | |
