4Y04
Crystal structure of dipeptidyl peptidase 11 (DPP11) from Porphyromonas gingivalis (Space)
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue K A 801 |
Chain | Residue |
A | ASN218 |
A | TRP219 |
A | ASP672 |
A | HOH1587 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue K A 802 |
Chain | Residue |
A | THR278 |
A | THR651 |
A | ASP681 |
A | HOH1059 |
A | HOH1429 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 803 |
Chain | Residue |
A | ASP60 |
A | PHE124 |
A | LYS194 |
A | PRO253 |
A | LYS254 |
A | ARG255 |
A | HOH965 |
A | HOH1432 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
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 | 1 |
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 | 1 |
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 |