3LXU
Crystal Structure of Tripeptidyl Peptidase 2 (TPP II)
Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0004177 | molecular_function | aminopeptidase activity |
X | 0004252 | molecular_function | serine-type endopeptidase activity |
X | 0005737 | cellular_component | cytoplasm |
X | 0005829 | cellular_component | cytosol |
X | 0006508 | biological_process | proteolysis |
X | 0008233 | molecular_function | peptidase activity |
X | 0008236 | molecular_function | serine-type peptidase activity |
X | 0008240 | molecular_function | tripeptidyl-peptidase activity |
X | 0016787 | molecular_function | hydrolase activity |
X | 0017171 | molecular_function | serine hydrolase activity |
X | 0032991 | cellular_component | protein-containing complex |
X | 0042802 | molecular_function | identical protein binding |
Functional Information from PROSITE/UniProt
site_id | PS00137 |
Number of Residues | 11 |
Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVSSiASG |
Chain | Residue | Details |
X | HIS272-GLY282 |
site_id | PS00138 |
Number of Residues | 11 |
Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAaPhVAG |
Chain | Residue | Details |
X | GLY460-GLY470 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 70 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20676100","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18327897","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |