Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1001 |
| Chain | Residue |
| A | ASP218 |
| A | ASP229 |
| A | GLU322 |
| A | GLU336 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A1002 |
| Chain | Residue |
| A | HOH1065 |
| A | LYS259 |
| A | THR351 |
| A | CL1006 |
| A | HOH1020 |
| A | HOH1022 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A1003 |
| Chain | Residue |
| A | GLU155 |
| A | LYS179 |
| A | GLU180 |
| A | HOH1223 |
| B | VAL359 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A1005 |
| Chain | Residue |
| A | PHE120 |
| A | ARG275 |
| A | ARG279 |
| A | HOH1173 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A1006 |
| Chain | Residue |
| A | LYS143 |
| A | LYS259 |
| A | LYS262 |
| A | NA1002 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A1007 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A1008 |
| Chain | Residue |
| A | ARG109 |
| A | HOH1361 |
| B | HOH1041 |
| B | HOH1054 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A1011 |
| Chain | Residue |
| A | GLY194 |
| A | GLY212 |
| A | VAL214 |
| A | VAL243 |
| A | HOH1076 |
| A | HOH1184 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B1004 |
| Chain | Residue |
| B | LYS65 |
| B | THR68 |
| B | HOH1162 |
| B | HOH1265 |
| B | HOH1355 |
Functional Information from PROSITE/UniProt
| site_id | PS00491 |
| Number of Residues | 13 |
| Details | PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HSLGHgIGLeVHE |
| Chain | Residue | Details |
| A | HIS289-GLU301 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | HIS300 | |
| A | GLU322 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| B | HIS300 | |
| B | GLU322 | |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU322 | |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| B | GLU322 | |
