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 | 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 | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue AMP A 401 |
| Chain | Residue |
| A | LYS104 |
| A | PHE214 |
| A | TYR215 |
| A | GLU275 |
| A | HOH602 |
| A | HOH635 |
| A | HOH648 |
| A | HOH665 |
| A | PRO119 |
| A | PHE146 |
| A | LYS148 |
| A | GLU184 |
| A | LYS185 |
| A | SER186 |
| A | ILE187 |
| A | GLU192 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | HIS70 |
| A | HOH501 |
| A | HOH505 |
| A | HOH642 |
| A | HOH683 |
| A | HOH712 |
| A | HOH850 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 405 |
| Chain | Residue |
| A | ARG293 |
| A | GLY298 |
| A | TYR299 |
| A | HOH570 |
| A | HOH593 |
| A | HOH616 |
| A | HOH639 |
| A | HOH756 |
| B | ARG293 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | GLN112 |
| A | PHE121 |
| A | HOH510 |
| A | HOH625 |
| A | HOH659 |
| B | GLN113 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | HIS45 |
| A | HOH528 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | ARG126 |
| A | LYS179 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| A | ARG293 |
| A | HOH630 |
| A | HOH942 |
| B | LYS290 |
| B | HOH532 |
| B | HOH605 |
| B | HOH630 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | ALA240 |
| B | ARG244 |
| B | EDO403 |
| B | HOH506 |
| B | HOH609 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | ALA236 |
| B | ALA237 |
| B | EDO402 |
| B | HOH515 |
| B | HOH520 |
| B | HOH543 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue AMP B 404 |
| Chain | Residue |
| B | LYS104 |
| B | PHE146 |
| B | LYS148 |
| B | SER155 |
| B | VAL158 |
| B | GLU184 |
| B | LYS185 |
| B | SER186 |
| B | ILE187 |
| B | GLU192 |
| B | PHE214 |
| B | TYR215 |
| B | LEU274 |
| B | GLU275 |
| B | HOH531 |
| B | HOH565 |
| B | HOH644 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 B 405 |
| Chain | Residue |
| B | HIS70 |
| B | TYR221 |
| B | ARG260 |
| B | ASN277 |
| B | PRO280 |
| B | GLY281 |
| B | HOH559 |
| B | HOH569 |
| B | HOH608 |
| B | HOH664 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue PGE B 406 |
| Chain | Residue |
| B | ARG293 |
| B | GLY298 |
| B | TYR299 |
| B | SER300 |
| B | GLU301 |
| B | HOH502 |
| B | HOH516 |
| B | HOH526 |
| B | HOH578 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| A | GLN112 |
| B | GLN113 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | HOH631 |
| B | HOH682 |
| B | ARG207 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 409 |
| Chain | Residue |
| B | VAL25 |
| B | SER29 |
| B | ALA68 |
| B | LEU69 |
| B | HIS70 |
| B | ALA279 |
| B | PRO280 |
| B | HOH545 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide DAL A 402 and DAL A 403 |
| Chain | Residue |
| A | HIS70 |
| A | ARG260 |
| A | ASN277 |
| A | GLY281 |
| A | SER286 |
| A | LEU287 |
| A | HOH523 |
Functional Information from PROSITE/UniProt
| site_id | PS00843 |
| Number of Residues | 12 |
| Details | DALA_DALA_LIGASE_1 D-alanine--D-alanine ligase signature 1. HGgyGENGqIQG |
| Chain | Residue | Details |
| A | HIS70-GLY81 | |
| site_id | PS00844 |
| Number of Residues | 29 |
| Details | DALA_DALA_LIGASE_2 D-alanine--D-alanine ligase signature 2. LgctDwGRADFMldaagnpy....FlEVNTaPG |
| Chain | Residue | Details |
| A | LEU253-GLY281 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 400 |
| Details | Domain: {"description":"ATP-grasp","evidences":[{"source":"HAMAP-Rule","id":"MF_00047","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 116 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00047","evidenceCode":"ECO:0000255"}]} |
