5JWF
Crystal structure of Porphyromonas gingivalis DPP11
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| A | 0009986 | cellular_component | cell surface |
| A | 0042277 | molecular_function | peptide binding |
| A | 0043171 | biological_process | peptide catabolic process |
| A | 0048588 | biological_process | developmental cell growth |
| A | 0070009 | molecular_function | serine-type aminopeptidase activity |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0008239 | molecular_function | dipeptidyl-peptidase activity |
| B | 0009986 | cellular_component | cell surface |
| B | 0042277 | molecular_function | peptide binding |
| B | 0043171 | biological_process | peptide catabolic process |
| B | 0048588 | biological_process | developmental cell growth |
| B | 0070009 | molecular_function | serine-type aminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 801 |
| Chain | Residue |
| B | ASP297 |
| B | ARG301 |
| B | MET396 |
| B | GLU467 |
| B | HOH913 |
| B | HOH932 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 802 |
| Chain | Residue |
| B | LYS254 |
| B | PHE124 |
| B | LYS194 |
| B | PRO253 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 803 |
| Chain | Residue |
| B | ASN218 |
| B | TRP219 |
| B | PHE671 |
| B | ASP672 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PGO B 804 |
| Chain | Residue |
| B | ARG391 |
| B | TYR394 |
| B | LEU542 |
| B | HOH988 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:26057589 |
| Chain | Residue | Details |
| A | HIS85 | |
| A | ASP227 | |
| B | HIS85 | |
| B | ASP227 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:21896480, ECO:0000305|PubMed:26057589 |
| Chain | Residue | Details |
| A | ALA655 | |
| B | ALA655 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Is essential for the Asp/Glu P1 specificity of DPP11; involved in the recognition of the Asp/Glu residue at the P1 position of substrate peptides => ECO:0000269|PubMed:26057589 |
| Chain | Residue | Details |
| A | ARG673 | |
| B | ARG673 |
