1HI9
Zn-dependent D-aminopeptidase DppA from Bacillus subtilis, a self-compartmentalizing protease.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004177 | molecular_function | aminopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004177 | molecular_function | aminopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0004177 | molecular_function | aminopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0008237 | molecular_function | metallopeptidase activity |
| E | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 300 |
| Chain | Residue |
| A | ASP8 |
| A | HIS104 |
| A | HIS115 |
| A | GLU133 |
| A | ZN301 |
| A | HOH2059 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 301 |
| Chain | Residue |
| A | ZN300 |
| A | HOH2059 |
| A | ASP8 |
| A | GLU10 |
| A | HIS60 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 300 |
| Chain | Residue |
| B | ASP8 |
| B | HIS104 |
| B | HIS115 |
| B | GLU133 |
| B | ZN301 |
| B | HOH2025 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 301 |
| Chain | Residue |
| B | ASP8 |
| B | GLU10 |
| B | HIS60 |
| B | ZN300 |
| B | HOH2025 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 300 |
| Chain | Residue |
| C | ASP8 |
| C | HIS104 |
| C | HIS115 |
| C | GLU133 |
| C | ZN301 |
| C | HOH2037 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 301 |
| Chain | Residue |
| C | ASP8 |
| C | GLU10 |
| C | HIS60 |
| C | ZN300 |
| C | HOH2037 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN D 300 |
| Chain | Residue |
| D | ASP8 |
| D | HIS104 |
| D | HIS115 |
| D | GLU133 |
| D | ZN301 |
| D | HOH2053 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 301 |
| Chain | Residue |
| D | ASP8 |
| D | GLU10 |
| D | HIS60 |
| D | ZN300 |
| D | HOH2053 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN E 300 |
| Chain | Residue |
| E | ASP8 |
| E | HIS104 |
| E | HIS115 |
| E | GLU133 |
| E | ZN301 |
| E | HOH2073 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 301 |
| Chain | Residue |
| E | ASP8 |
| E | GLU10 |
| E | HIS60 |
| E | ZN300 |
| E | HOH2073 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | HIS115 | |
| B | HIS115 | |
| C | HIS115 | |
| D | HIS115 | |
| E | HIS115 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 25 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP8 | |
| B | GLU133 | |
| C | ASP8 | |
| C | GLU10 | |
| C | HIS60 | |
| C | HIS104 | |
| C | GLU133 | |
| D | ASP8 | |
| D | GLU10 | |
| D | HIS60 | |
| D | HIS104 | |
| A | GLU10 | |
| D | GLU133 | |
| E | ASP8 | |
| E | GLU10 | |
| E | HIS60 | |
| E | HIS104 | |
| E | GLU133 | |
| A | HIS60 | |
| A | HIS104 | |
| A | GLU133 | |
| B | ASP8 | |
| B | GLU10 | |
| B | HIS60 | |
| B | HIS104 |
