Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004185 | molecular_function | serine-type carboxypeptidase activity |
A | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | CAT |
Number of Residues | 4 |
Details | |
Chain | Residue |
A | SER146 |
A | ASP338 |
A | HIS397 |
A | GLU145 |
site_id | CBS |
Number of Residues | 4 |
Details | |
Chain | Residue |
A | ASN51 |
A | GLY52 |
A | GLU145 |
A | HIS397 |
site_id | S1P |
Number of Residues | 7 |
Details | |
Chain | Residue |
A | PHE64 |
A | GLU65 |
A | TYR256 |
A | TYR269 |
A | LEU272 |
A | MET398 |
A | THR60 |
site_id | S1S |
Number of Residues | 6 |
Details | |
Chain | Residue |
A | TYR147 |
A | LEU178 |
A | LEU245 |
A | TRP312 |
A | ILE340 |
A | CYS341 |
Functional Information from PROSITE/UniProt
site_id | PS00131 |
Number of Residues | 8 |
Details | CARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. IaGESYAG |
Chain | Residue | Details |
A | ILE142-GLY149 | |
site_id | PS00560 |
Number of Residues | 18 |
Details | CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. FtyLrVfNGGHmVPfdvP |
Chain | Residue | Details |
A | PHE387-PRO404 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER146 | |
Chain | Residue | Details |
A | ASP338 | |
Chain | Residue | Details |
A | HIS397 | |
Chain | Residue | Details |
A | CYS341 | |
A | MET398 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:28189789 |
Chain | Residue | Details |
A | ASN13 | |
Chain | Residue | Details |
A | ASN87 | |
A | ASN168 | |
A | ASN368 | |