3EDY
Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004175 | molecular_function | endopeptidase activity |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005764 | cellular_component | lysosome |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0006508 | biological_process | proteolysis |
A | 0006629 | biological_process | lipid metabolic process |
A | 0007040 | biological_process | lysosome organization |
A | 0007399 | biological_process | nervous system development |
A | 0007417 | biological_process | central nervous system development |
A | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0008240 | molecular_function | tripeptidyl-peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0030163 | biological_process | protein catabolic process |
A | 0030855 | biological_process | epithelial cell differentiation |
A | 0035727 | molecular_function | lysophosphatidic acid binding |
A | 0042277 | molecular_function | peptide binding |
A | 0042470 | cellular_component | melanosome |
A | 0043171 | biological_process | peptide catabolic process |
A | 0043202 | cellular_component | lysosomal lumen |
A | 0045121 | cellular_component | membrane raft |
A | 0045453 | biological_process | bone resorption |
A | 0046872 | molecular_function | metal ion binding |
A | 0050885 | biological_process | neuromuscular process controlling balance |
A | 0055037 | cellular_component | recycling endosome |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070198 | biological_process | protein localization to chromosome, telomeric region |
A | 0120146 | molecular_function | sulfatide binding |
A | 1905146 | biological_process | lysosomal protein catabolic process |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 |
Chain | Residue | Details |
A | GLU272 | |
A | ASP276 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Charge relay system => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000305|PubMed:11054422 |
Chain | Residue | Details |
A | SER475 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 |
Chain | Residue | Details |
A | ASP517 | |
A | GLY539 | |
A | GLY541 | |
A | ASP543 | |
A | VAL518 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN210 | |
A | ASN313 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN222 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967 |
Chain | Residue | Details |
A | ASN286 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN443 |