5JWG
Crystal structure of Porphyromonas endodontalis DPP11 in complex with dipeptide Arg-Asp
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| 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 | 0043171 | biological_process | peptide catabolic process |
| A | 0070009 | molecular_function | serine-type aminopeptidase activity |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0005576 | cellular_component | extracellular region |
| 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 | 0043171 | biological_process | peptide catabolic process |
| B | 0070009 | molecular_function | serine-type aminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ARG A 801 |
| Chain | Residue |
| A | HIS85 |
| A | ASP802 |
| A | HOH929 |
| A | HOH976 |
| A | HOH1128 |
| A | SER213 |
| A | ASN217 |
| A | TRP218 |
| A | ALA328 |
| A | GLN331 |
| A | ASN332 |
| A | PHE668 |
| A | ASP669 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue ASP A 802 |
| Chain | Residue |
| A | HIS85 |
| A | TRP218 |
| A | THR648 |
| A | GLY649 |
| A | GLY650 |
| A | ASN651 |
| A | ALA652 |
| A | PHE668 |
| A | ARG670 |
| A | ARG801 |
| A | HOH909 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 803 |
| Chain | Residue |
| A | GLU359 |
| A | ALA362 |
| A | TRP363 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 804 |
| Chain | Residue |
| A | THR371 |
| A | THR372 |
| A | SER552 |
| A | SER556 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue ARG B 801 |
| Chain | Residue |
| B | HIS85 |
| B | SER213 |
| B | ASN217 |
| B | TRP218 |
| B | ALA328 |
| B | GLN331 |
| B | ASN332 |
| B | PHE668 |
| B | ASP669 |
| B | ASP802 |
| B | HOH948 |
| B | HOH1009 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue ASP B 802 |
| Chain | Residue |
| B | HIS85 |
| B | TRP218 |
| B | THR648 |
| B | GLY649 |
| B | GLY650 |
| B | ASN651 |
| B | ALA652 |
| B | PHE668 |
| B | ARG670 |
| B | ARG801 |
| B | HOH907 |
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"}]} |
| 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"}]} |
| 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":"UniProtKB","id":"B2RID1","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"21896480","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
