7XNM

Structure of porcine dipeptidyl peptidase 4 inhibitory peptide complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001618	molecular_function	virus receptor activity
A	0001666	biological_process	response to hypoxia
A	0002020	molecular_function	protease binding
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005102	molecular_function	signaling receptor binding
A	0005576	cellular_component	extracellular region
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008236	molecular_function	serine-type peptidase activity
A	0008239	molecular_function	dipeptidyl-peptidase activity
A	0008240	molecular_function	tripeptidyl-peptidase activity
A	0008284	biological_process	positive regulation of cell population proliferation
A	0009986	cellular_component	cell surface
A	0010716	biological_process	negative regulation of extracellular matrix disassembly
A	0016324	cellular_component	apical plasma membrane
A	0030027	cellular_component	lamellipodium
A	0030139	cellular_component	endocytic vesicle
A	0031258	cellular_component	lamellipodium membrane
A	0031295	biological_process	T cell costimulation
A	0033632	biological_process	regulation of cell-cell adhesion mediated by integrin
A	0042110	biological_process	T cell activation
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043542	biological_process	endothelial cell migration
A	0045121	cellular_component	membrane raft
A	0045499	molecular_function	chemorepellent activity
A	0046581	cellular_component	intercellular canaliculus
A	0046718	biological_process	symbiont entry into host cell
A	0050919	biological_process	negative chemotaxis
A	0070161	cellular_component	anchoring junction
A	0090024	biological_process	negative regulation of neutrophil chemotaxis
B	0001618	molecular_function	virus receptor activity
B	0001666	biological_process	response to hypoxia
B	0002020	molecular_function	protease binding
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005102	molecular_function	signaling receptor binding
B	0005576	cellular_component	extracellular region
B	0005886	cellular_component	plasma membrane
B	0006508	biological_process	proteolysis
B	0008236	molecular_function	serine-type peptidase activity
B	0008239	molecular_function	dipeptidyl-peptidase activity
B	0008240	molecular_function	tripeptidyl-peptidase activity
B	0008284	biological_process	positive regulation of cell population proliferation
B	0009986	cellular_component	cell surface
B	0010716	biological_process	negative regulation of extracellular matrix disassembly
B	0016324	cellular_component	apical plasma membrane
B	0030027	cellular_component	lamellipodium
B	0030139	cellular_component	endocytic vesicle
B	0031258	cellular_component	lamellipodium membrane
B	0031295	biological_process	T cell costimulation
B	0033632	biological_process	regulation of cell-cell adhesion mediated by integrin
B	0042110	biological_process	T cell activation
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043542	biological_process	endothelial cell migration
B	0045121	cellular_component	membrane raft
B	0045499	molecular_function	chemorepellent activity
B	0046581	cellular_component	intercellular canaliculus
B	0046718	biological_process	symbiont entry into host cell
B	0050919	biological_process	negative chemotaxis
B	0070161	cellular_component	anchoring junction
B	0090024	biological_process	negative regulation of neutrophil chemotaxis

Functional Information from PROSITE/UniProt

site_id	PS00708
Number of Residues	31
Details	PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAtrqFskmgfvddkriaiwGwSyGGYV

Chain	Residue	Details
A	ASP605-VAL635

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12690074","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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