Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0016805 | molecular_function | dipeptidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0102009 | molecular_function | proline dipeptidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0016805 | molecular_function | dipeptidase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0102009 | molecular_function | proline dipeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CAC A 403 |
| Chain | Residue |
| A | PHE181 |
| A | ASP212 |
| A | ASP223 |
| A | HIS294 |
| A | GLU316 |
| A | GLU330 |
| A | ZN405 |
| A | ZN406 |
| A | HOH1743 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CAC B 404 |
| Chain | Residue |
| B | PHE181 |
| B | ASP212 |
| B | ASP223 |
| B | VAL293 |
| B | HIS294 |
| B | GLU316 |
| B | GLU330 |
| B | ZN407 |
| B | ZN408 |
| B | HOH548 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 405 |
| Chain | Residue |
| A | ASP212 |
| A | ASP223 |
| A | THR225 |
| A | GLU330 |
| A | CAC403 |
| A | ZN406 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 406 |
| Chain | Residue |
| A | ASP223 |
| A | HIS287 |
| A | GLU316 |
| A | GLU330 |
| A | CAC403 |
| A | ZN405 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 407 |
| Chain | Residue |
| B | ASP212 |
| B | ASP223 |
| B | THR225 |
| B | GLU330 |
| B | CAC404 |
| B | ZN408 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 408 |
| Chain | Residue |
| B | ASP223 |
| B | HIS287 |
| B | GLU316 |
| B | GLU330 |
| B | CAC404 |
| B | ZN407 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1409 |
| Chain | Residue |
| A | HOH1424 |
| A | HOH1518 |
| A | HOH1613 |
| A | HOH1647 |
| A | HOH1746 |
| A | HOH1747 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1401 |
| Chain | Residue |
| A | LYS27 |
| A | ASN30 |
| A | GLU94 |
| A | SER95 |
| A | SER96 |
| A | ASP118 |
| A | ARG125 |
| A | TRP296 |
| A | GOL1402 |
| A | HOH1491 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1402 |
| Chain | Residue |
| A | LYS27 |
| A | ARG125 |
| A | GLU292 |
| A | TRP296 |
| A | GOL1401 |
| A | HOH1717 |
Functional Information from PROSITE/UniProt
| site_id | PS00491 |
| Number of Residues | 13 |
| Details | PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HSLGHgVGLeVHE |
| Chain | Residue | Details |
| A | HIS283-GLU295 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP212 | |
| B | GLU330 | |
| A | ASP223 | |
| A | HIS287 | |
| A | GLU316 | |
| A | GLU330 | |
| B | ASP212 | |
| B | ASP223 | |
| B | HIS287 | |
| B | GLU316 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU316 | |
| A | HIS294 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| B | GLU316 | |
| B | HIS294 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU316 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| B | GLU316 | |
