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 | 0008235 | molecular_function | metalloexopeptidase activity |
A | 0008237 | molecular_function | metallopeptidase 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 | 6 |
Details | BINDING SITE FOR RESIDUE MN A 443 |
Chain | Residue |
A | GLU406 |
A | MN444 |
A | HOH790 |
A | ASP271 |
A | HIS354 |
A | GLU383 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MN A 444 |
Chain | Residue |
A | TYR229 |
A | ASP260 |
A | ASP271 |
A | THR273 |
A | GLU406 |
A | MN443 |
A | HOH473 |
A | HOH790 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR DIPEPTIDE PRO-LEU OF LINKED RESIDUES A 441 to 442 |
Chain | Residue |
A | TRP88 |
A | ARG153 |
A | HIS243 |
A | HIS350 |
A | GLY351 |
A | HIS354 |
A | HIS361 |
A | ARG370 |
A | GLU383 |
A | ARG404 |
A | HOH786 |
A | HOH787 |
A | HOH788 |
A | HOH790 |
site_id | NUL |
Number of Residues | 6 |
Details | THESE RESIDUES COORDINATE THE MN IONS. |
Chain | Residue |
A | ASP260 |
A | ASP271 |
A | HIS354 |
A | GLU383 |
A | GLU406 |
A | HOH784 |
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 | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 9520390, 8849731 |
Chain | Residue | Details |
A | HIS361 | |
A | GLU383 | |
A | HIS243 | |
A | HIS350 | |
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) |