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 | 21 |
Details | BINDING SITE FOR RESIDUE ADP A 401 |
Chain | Residue |
A | LYS140 |
A | GLU226 |
A | LEU247 |
A | TYR258 |
A | LYS261 |
A | PHE301 |
A | ASN311 |
A | GLU312 |
A | HOH556 |
A | HOH588 |
A | HOH593 |
A | PHE181 |
A | HOH637 |
B | TYR258 |
A | LYS183 |
A | SER190 |
A | ILE193 |
A | GLU219 |
A | GLU220 |
A | THR221 |
A | ILE222 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 402 |
Chain | Residue |
A | ARG297 |
A | ASN314 |
A | PRO317 |
A | GLY318 |
A | HOH501 |
A | HOH525 |
A | HOH575 |
B | LYS257 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | ASN223 |
A | THR303 |
A | PRO304 |
A | SER305 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 404 |
Chain | Residue |
A | SER335 |
A | PHE336 |
A | HOH611 |
A | HOH612 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 405 |
Chain | Residue |
A | LYS108 |
A | GLY188 |
A | SER189 |
A | HOH640 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP B 401 |
Chain | Residue |
B | PHE181 |
B | LYS183 |
B | SER190 |
B | ILE193 |
B | GLU219 |
B | GLU220 |
B | THR221 |
B | ILE222 |
B | GLU226 |
B | LEU247 |
B | PHE252 |
B | PHE301 |
B | ASN311 |
B | GLU312 |
B | HOH503 |
B | HOH529 |
B | HOH540 |
B | HOH617 |
B | HOH649 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 402 |
Chain | Residue |
B | ARG297 |
B | GLY318 |
B | SER323 |
B | ARG324 |
B | HOH501 |
B | HOH514 |
B | HOH633 |
B | HOH641 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 403 |
Chain | Residue |
B | ASN223 |
B | THR303 |
B | PRO304 |
B | SER305 |
B | HOH594 |
B | HOH600 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 404 |
Chain | Residue |
A | TYR254 |
B | ALA187 |
B | GLY188 |
B | SER189 |
B | HIS212 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 405 |
Chain | Residue |
A | LYS330 |
B | LYS264 |
B | TYR266 |
B | ARG270 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 406 |
Chain | Residue |
B | LYS330 |
B | SER335 |
B | PHE336 |
Functional Information from PROSITE/UniProt
site_id | PS00843 |
Number of Residues | 12 |
Details | DALA_DALA_LIGASE_1 D-alanine--D-alanine ligase signature 1. HGknGEDGtLQG |
Chain | Residue | Details |
A | HIS106-GLY117 | |
site_id | PS00844 |
Number of Residues | 29 |
Details | DALA_DALA_LIGASE_2 D-alanine--D-alanine ligase signature 2. LgcsGfSRVDMFytpsgeiv....FnEVNTiPG |
Chain | Residue | Details |
A | LEU290-GLY318 | |