Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004185 | molecular_function | serine-type carboxypeptidase activity |
A | 0006508 | biological_process | proteolysis |
B | 0004185 | molecular_function | serine-type carboxypeptidase activity |
B | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | CAT |
Number of Residues | 3 |
Details | THREE RESIDUES FORMING THE CATALYTIC CENTER |
Chain | Residue |
B | ASP338 |
B | HIS397 |
A | SER146 |
Functional Information from PROSITE/UniProt
site_id | PS00560 |
Number of Residues | 18 |
Details | CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. LtlVsVrGAGHeVPlhrP |
Chain | Residue | Details |
B | LEU387-PRO404 | |
site_id | PS00131 |
Number of Residues | 8 |
Details | CARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. IaGESYAG |
Chain | Residue | Details |
A | ILE142-GLY149 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | THR367 | |
B | LYS418 | |
Chain | Residue | Details |
B | PHE414 | |
A | GLU145 | |
Chain | Residue | Details |
B | HIS308 | |
A | ASN113 | |
Chain | Residue | Details |
B | MET313 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 5 |
Chain | Residue | Details |
B | THR367 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
B | LYS418 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | TYR147 | electrostatic stabiliser, hydrogen bond donor |