Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005515 | molecular_function | protein 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 | 0008765 | molecular_function | UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0016881 | molecular_function | acid-amino acid ligase activity |
A | 0051301 | biological_process | cell division |
A | 0071555 | biological_process | cell wall organization |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0005515 | molecular_function | protein 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 | 0008765 | molecular_function | UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0016881 | molecular_function | acid-amino acid ligase activity |
B | 0051301 | biological_process | cell division |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue LVV A 501 |
Chain | Residue |
A | PHE204 |
A | LEU253 |
A | LYS351 |
A | ARG489 |
A | LEU490 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue LVV A 502 |
Chain | Residue |
A | VAL165 |
A | GLU168 |
A | GLU183 |
A | SER185 |
A | GLY188 |
A | VAL194 |
A | ASN146 |
A | THR155 |
A | THR158 |
A | GLY160 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue DMS A 503 |
Chain | Residue |
A | GLY113 |
A | VAL184 |
A | SER202 |
A | TYR229 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue DMS A 504 |
Chain | Residue |
A | ARG110 |
A | LEU322 |
A | GLY323 |
A | TYR324 |
B | ASP107 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue LVV B 501 |
Chain | Residue |
B | PHE204 |
B | LEU253 |
B | LYS351 |
B | ARG489 |
B | LEU490 |
B | GLY492 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue LVV B 502 |
Chain | Residue |
B | ASN146 |
B | GLU183 |
B | SER185 |
B | GLY188 |
B | VAL194 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue DMS B 503 |
Chain | Residue |
B | THR115 |
B | VAL184 |
B | LEU189 |
B | SER202 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 24 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU27 | |
A | ASP414 | |
A | GLY465 | |
A | GLU469 | |
B | LEU27 | |
B | SER29 | |
B | HIS44 | |
B | ASN157 | |
B | THR158 | |
B | SER185 | |
B | GLN191 | |
A | SER29 | |
B | ARG193 | |
B | ARG390 | |
B | ASP414 | |
B | GLY465 | |
B | GLU469 | |
A | HIS44 | |
A | ASN157 | |
A | THR158 | |
A | SER185 | |
A | GLN191 | |
A | ARG193 | |
A | ARG390 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY116 | |
B | GLY116 | |
Chain | Residue | Details |
A | LYS225 | |
B | LYS225 | |