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	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

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site_id	PS00138
Number of Residues	11
Details	SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAaPhVAG

Chain	Residue	Details
X	GLY460-GLY470

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:20676100

Chain	Residue	Details
X	ASP44
X	HIS272
X	SER462

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:18327897

Chain	Residue	Details
X	SER1095

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