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3EDY

Crystal Structure of the Precursor Form of Human Tripeptidyl-Peptidase 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005764cellular_componentlysosome
A0005794cellular_componentGolgi apparatus
A0006508biological_processproteolysis
A0006629biological_processlipid metabolic process
A0007040biological_processlysosome organization
A0007399biological_processnervous system development
A0007417biological_processcentral nervous system development
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0008240molecular_functiontripeptidyl-peptidase activity
A0016787molecular_functionhydrolase activity
A0030163biological_processprotein catabolic process
A0030855biological_processepithelial cell differentiation
A0035727molecular_functionlysophosphatidic acid binding
A0042277molecular_functionpeptide binding
A0042470cellular_componentmelanosome
A0043171biological_processpeptide catabolic process
A0043202cellular_componentlysosomal lumen
A0045121cellular_componentmembrane raft
A0045453biological_processbone resorption
A0046872molecular_functionmetal ion binding
A0050885biological_processneuromuscular process controlling balance
A0055037cellular_componentrecycling endosome
A0070062cellular_componentextracellular exosome
A0070198biological_processprotein localization to chromosome, telomeric region
A0120146molecular_functionsulfatide binding
A1905146biological_processlysosomal protein catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967
ChainResidueDetails
AGLU272
AASP276

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000305|PubMed:11054422
ChainResidueDetails
ASER475

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967
ChainResidueDetails
AASP517
AGLY539
AGLY541
AASP543
AVAL518

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN210
AASN313

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN222

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967
ChainResidueDetails
AASN286

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19038966, ECO:0000269|PubMed:19038967, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN443

218500

PDB entries from 2024-04-17

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