Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000270 | biological_process | peptidoglycan metabolic process |
A | 0008933 | molecular_function | lytic transglycosylase activity |
A | 0016020 | cellular_component | membrane |
A | 0016837 | molecular_function | carbon-oxygen lyase activity, acting on polysaccharides |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG A 501 |
Chain | Residue |
A | ASP88 |
A | HOH618 |
A | HOH644 |
A | HOH668 |
A | HOH733 |
A | HOH943 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | HOH697 |
A | HOH698 |
A | HOH725 |
A | HOH629 |
A | HOH661 |
A | HOH682 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CL A 503 |
Chain | Residue |
A | TRP410 |
A | LYS414 |
A | GLN444 |
A | ARG447 |
Functional Information from PROSITE/UniProt
site_id | PS00922 |
Number of Residues | 29 |
Details | TRANSGLYCOSYLASE Prokaryotic transglycosylases signature. IgyqESlwqPgatSktgvrGLMmLtnrtA |
Chain | Residue | Details |
A | ILE312-ALA340 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU316 | |