Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008235 | molecular_function | metalloexopeptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 601 |
| Chain | Residue |
| A | ARG79 |
| A | VAL80 |
| A | SER111 |
| A | HOH1058 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PG4 A 701 |
| Chain | Residue |
| A | ASP271 |
| A | VAL360 |
| A | HIS361 |
| A | GLU383 |
| A | ARG404 |
| A | HOH988 |
| A | TYR229 |
| A | ILE232 |
| A | LEU242 |
| A | HIS243 |
| A | ASP260 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IPA A 702 |
| Chain | Residue |
| A | ILE27 |
| A | PHE28 |
| A | ASN46 |
| A | TRP165 |
| A | HOH717 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IPA A 703 |
| Chain | Residue |
| A | ARG149 |
| A | PRO159 |
| A | ALA160 |
| A | MET162 |
| A | HOH758 |
Functional Information from PROSITE/UniProt
| site_id | PS00491 |
| Number of Residues | 13 |
| Details | PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLSHwLGLdVHD |
| Chain | Residue | Details |
| A | HIS350-ASP362 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Binding site: {} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU383 | |
| A | HIS361 | |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a16 |
| Chain | Residue | Details |
| A | GLU383 | |
| site_id | MCSA1 |
| Number of Residues | 11 |
| Details | M-CSA 379 |
| Chain | Residue | Details |
| A | ASP38 | activator, electrostatic stabiliser |
| A | ARG404 | proton shuttle (general acid/base) |
| A | GLU406 | metal ligand |
| A | HIS243 | electrostatic stabiliser |
| A | ASP260 | metal ligand, proton shuttle (general acid/base) |
| A | ASP271 | metal ligand |
| A | HIS350 | electrostatic stabiliser |
| A | HIS354 | metal ligand |
| A | HIS361 | electrostatic stabiliser |
| A | GLU383 | activator, metal ligand, proton shuttle (general acid/base) |
| A | TYR387 | proton shuttle (general acid/base) |
