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 | 0046914 | molecular_function | transition 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 | 7 |
| Details | BINDING SITE FOR RESIDUE MN A 2001 |
| Chain | Residue |
| A | ASP271 |
| A | HIS354 |
| A | THR381 |
| A | GLU383 |
| A | GLU406 |
| A | MN2002 |
| B | 01B1 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN A 2002 |
| Chain | Residue |
| A | ASP271 |
| A | THR273 |
| A | GLU406 |
| A | MN2001 |
| B | 01B1 |
| A | TYR229 |
| A | ASP260 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 2003 |
| Chain | Residue |
| A | HOH2163 |
| A | HOH2166 |
| A | HOH2171 |
| A | HOH2172 |
| A | HOH2173 |
| A | HOH2174 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR CHAIN B OF APSTATIN |
| Chain | Residue |
| A | TRP88 |
| A | TYR229 |
| A | HIS243 |
| A | ASP260 |
| A | ASP271 |
| A | HIS350 |
| A | HIS354 |
| A | HIS361 |
| A | GLU383 |
| A | ARG404 |
| A | GLU406 |
| A | MN2001 |
| A | MN2002 |
| A | HOH2222 |
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: |
| Chain | Residue | Details |
| A | ALA261 | |
| A | ILE272 | |
| A | TRP355 | |
| A | PRO384 | |
| A | ASP407 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 11 |
| Details | M-CSA 379 |
| Chain | Residue | Details |
| A | SER39 | activator, electrostatic stabiliser |
| A | ILE405 | proton shuttle (general acid/base) |
| A | ASP407 | metal ligand |
| A | TYR244 | electrostatic stabiliser |
| A | ALA261 | metal ligand, proton shuttle (general acid/base) |
| A | ILE272 | metal ligand |
| A | GLY351 | electrostatic stabiliser |
| A | TRP355 | metal ligand |
| A | ASP362 | electrostatic stabiliser |
| A | PRO384 | activator, metal ligand, proton shuttle (general acid/base) |
| A | ILE388 | proton shuttle (general acid/base) |
