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 | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
A | 0009986 | cellular_component | cell surface |
A | 0016787 | molecular_function | hydrolase activity |
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 | 0008233 | molecular_function | peptidase activity |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0008239 | molecular_function | dipeptidyl-peptidase activity |
B | 0009986 | cellular_component | cell surface |
B | 0016787 | molecular_function | hydrolase activity |
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 | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"V5YM14","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"26057589","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"V5YM14","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"21896480","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26057589","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Site: {"description":"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","evidences":[{"source":"PubMed","id":"26057589","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |