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 |
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
Chain | Residue | Details |
A | GLU275 | |
A | ASN277 | |
B | VAL138 | |
B | ASP262 | |
B | GLU275 | |
B | ASN277 | |
A | VAL138 | |
A | ASP262 | |