3EAG
The crystal structure of UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase (MPL) from Neisseria meningitides
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0009058 | biological_process | biosynthetic process |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016881 | molecular_function | acid-amino acid ligase activity |
A | 0071555 | biological_process | cell wall organization |
B | 0005524 | molecular_function | ATP binding |
B | 0009058 | biological_process | biosynthetic process |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016881 | molecular_function | acid-amino acid ligase activity |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 401 |
Chain | Residue |
A | PRO89 |
A | TYR90 |
A | ILE91 |
A | GLN95 |
A | HOH427 |
B | HIS103 |
B | ARG188 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 401 |
Chain | Residue |
A | ARG188 |
B | PRO89 |
B | TYR90 |
A | GLU99 |
A | HIS103 |