3KHZ
Crystal Structure of R350A mutant of Staphylococcus aureus metallopeptidase (Sapep/DapE) in the apo-form
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016805 | molecular_function | dipeptidase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016805 | molecular_function | dipeptidase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | ASP86 | |
B | ASP86 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | GLU149 | |
B | GLU149 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS84 | |
B | HIS440 | |
A | ASP115 | |
A | GLU150 | |
A | ASP173 | |
A | HIS440 | |
B | HIS84 | |
B | ASP115 | |
B | GLU150 | |
B | ASP173 |