6HP8
Crystal structure of DPP8 in complex with Val-BoroPro
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006508 | biological_process | proteolysis |
A | 0006915 | biological_process | apoptotic process |
A | 0006955 | biological_process | immune response |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0008239 | molecular_function | dipeptidyl-peptidase activity |
A | 0043069 | biological_process | negative regulation of programmed cell death |
B | 0004177 | molecular_function | aminopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006508 | biological_process | proteolysis |
B | 0006915 | biological_process | apoptotic process |
B | 0006955 | biological_process | immune response |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0008239 | molecular_function | dipeptidyl-peptidase activity |
B | 0043069 | biological_process | negative regulation of programmed cell death |
C | 0004177 | molecular_function | aminopeptidase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006508 | biological_process | proteolysis |
C | 0006915 | biological_process | apoptotic process |
C | 0006955 | biological_process | immune response |
C | 0008236 | molecular_function | serine-type peptidase activity |
C | 0008239 | molecular_function | dipeptidyl-peptidase activity |
C | 0043069 | biological_process | negative regulation of programmed cell death |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue GK2 A 901 |
Chain | Residue |
A | ARG160 |
A | ASN835 |
A | HIS865 |
A | GLU275 |
A | GLU276 |
A | TYR669 |
A | GLN673 |
A | SER755 |
A | TYR756 |
A | TYR787 |
A | TYR791 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue NA A 902 |
Chain | Residue |
A | ARG158 |
A | GLN274 |
A | GLU275 |
A | ASP278 |
A | TYR280 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL A 903 |
Chain | Residue |
A | HIS315 |
A | THR317 |
A | ARG324 |
A | ALA326 |
A | PHE831 |
A | HIS837 |
A | HOH1083 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 904 |
Chain | Residue |
A | HIS188 |
A | LEU206 |
A | GLU208 |
A | ILE241 |
A | HOH1003 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue GOL A 905 |
Chain | Residue |
A | GLY526 |
A | SER527 |
A | ASN528 |
A | ILE529 |
A | GLN530 |
A | GLU541 |
A | CYS575 |
A | ILE577 |
A | HOH1014 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL A 906 |
Chain | Residue |
A | ASN448 |
A | HIS525 |
A | GLN673 |
A | HOH1031 |
A | HOH1102 |
A | HOH1166 |
A | HOH1201 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue GOL A 907 |
Chain | Residue |
A | TRP383 |
A | THR384 |
A | PRO385 |
A | TRP391 |
A | PHE453 |
A | VAL455 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue NA B 902 |
Chain | Residue |
B | ARG158 |
B | GLN274 |
B | ASP278 |
B | TYR280 |
B | HOH1131 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL B 903 |
Chain | Residue |
B | THR317 |
B | ARG324 |
B | ARG325 |
C | HIS315 |
C | HIS837 |
C | GOL903 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue GOL B 904 |
Chain | Residue |
A | HOH1011 |
B | HIS188 |
B | LEU206 |
B | GLU208 |
B | ILE241 |
B | ARG244 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 905 |
Chain | Residue |
B | TRP383 |
B | TRP391 |
B | PHE453 |
B | HIS454 |
B | VAL455 |
B | HOH1002 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue GOL B 906 |
Chain | Residue |
B | ASN448 |
B | ILE449 |
B | ARG524 |
B | GLN673 |
B | ARG794 |
B | HOH1025 |
B | HOH1051 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue GOL B 907 |
Chain | Residue |
B | GLY526 |
B | SER527 |
B | ASN528 |
B | GLN530 |
B | GLU541 |
B | CYS575 |
B | ILE577 |
B | HOH1174 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue NA C 902 |
Chain | Residue |
C | ARG158 |
C | GLN274 |
C | ASP278 |
C | TYR280 |
C | HOH1007 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue GOL C 903 |
Chain | Residue |
C | ALA326 |
C | PHE831 |
B | HIS315 |
B | HIS837 |
B | GOL903 |
B | HOH1115 |
C | THR317 |
C | ARG324 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue GOL C 904 |
Chain | Residue |
C | TRP383 |
C | TRP391 |
C | PHE453 |
C | HIS454 |
C | VAL455 |
site_id | AD8 |
Number of Residues | 10 |
Details | binding site for residue GOL C 905 |
Chain | Residue |
C | ASN448 |
C | ARG524 |
C | HIS525 |
C | GLN673 |
C | ARG794 |
C | HOH1004 |
C | HOH1030 |
C | HOH1067 |
C | HOH1123 |
C | HOH1166 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue GOL C 906 |
Chain | Residue |
C | GLY526 |
C | SER527 |
C | ASN528 |
C | GLU541 |
C | CYS575 |
C | ILE577 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue GOL C 907 |
Chain | Residue |
C | HIS595 |
C | LYS682 |
site_id | AE2 |
Number of Residues | 17 |
Details | binding site for Di-peptide GK2 B 901 and SER B 755 |
Chain | Residue |
B | ARG160 |
B | GLU275 |
B | GLU276 |
B | TYR669 |
B | GLN673 |
B | TRP754 |
B | TYR756 |
B | GLY757 |
B | GLY758 |
B | TYR759 |
B | GLY778 |
B | ALA779 |
B | PRO780 |
B | TYR787 |
B | TYR791 |
B | ASN835 |
B | HIS865 |
site_id | AE3 |
Number of Residues | 17 |
Details | binding site for Di-peptide GK2 C 901 and SER C 755 |
Chain | Residue |
C | ARG160 |
C | GLU275 |
C | GLU276 |
C | TYR669 |
C | GLN673 |
C | TRP754 |
C | TYR756 |
C | GLY757 |
C | GLY758 |
C | TYR759 |
C | GLY778 |
C | ALA779 |
C | TYR787 |
C | TYR791 |
C | ASN835 |
C | HIS865 |
C | HOH1150 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | ACT_SITE: Charge relay system => ECO:0000305|PubMed:12534281, ECO:0000305|PubMed:29382749 |
Chain | Residue | Details |
A | SER755 | |
A | ASP833 | |
A | HIS865 | |
B | SER755 | |
B | ASP833 | |
B | HIS865 | |
C | SER755 | |
C | ASP833 | |
C | HIS865 |