5JWI
Crystal structure of Porphyromonas endodontalis DPP11 in complex with dipeptide Arg-Glu
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 | 0008236 | molecular_function | serine-type peptidase activity |
A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
A | 0009986 | cellular_component | cell surface |
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 | 0008236 | molecular_function | serine-type peptidase activity |
B | 0008239 | molecular_function | dipeptidyl-peptidase activity |
B | 0009986 | cellular_component | cell surface |
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 | GLU802 |
A | HOH1071 |
A | HOH1079 |
A | HOH1134 |
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 GLU A 802 |
Chain | Residue |
A | HIS85 |
A | THR647 |
A | THR648 |
A | GLY649 |
A | GLY650 |
A | ALA652 |
A | ASN667 |
A | PHE668 |
A | ASP669 |
A | ARG670 |
A | ARG801 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CL B 801 |
Chain | Residue |
B | VAL263 |
B | LYS595 |
B | ASN632 |
B | ARG694 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CL B 802 |
Chain | Residue |
B | LEU682 |
B | PRO683 |
B | ASN684 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue ARG B 803 |
Chain | Residue |
B | SER213 |
B | ASN217 |
B | TRP218 |
B | ALA328 |
B | ASN332 |
B | ASP669 |
B | GLU804 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue GLU B 804 |
Chain | Residue |
B | HIS85 |
B | THR647 |
B | THR648 |
B | GLY649 |
B | GLY650 |
B | ASN651 |
B | ALA652 |
B | ASN667 |
B | PHE668 |
B | ASP669 |
B | ARG670 |
B | ARG803 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14 |
Chain | Residue | Details |
A | HIS85 | |
A | ASP226 | |
B | HIS85 | |
B | ASP226 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:21896480 |
Chain | Residue | Details |
A | ALA652 | |
B | ALA652 |
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:0000250|UniProtKB:B2RID1, ECO:0000305|PubMed:21896480 |
Chain | Residue | Details |
A | ARG670 | |
B | ARG670 |