3N0T

Human dipeptidil peptidase DPP7 complexed with inhibitor GSK237826A

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Peptidase_S28_2nd	e3n0tA2	A: alpha arrays	X: Dipeptidyl-peptidase 2 helical domain (From Topology)	H: Dipeptidyl-peptidase 2 helical domain (From Topology)	T: Dipeptidyl-peptidase 2 helical domain	F: Peptidase_S28_2nd	ECOD (1.6)
A	Peptidase_S28_1st	e3n0tA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Peptidase_S28_1st	ECOD (1.6)
B	Peptidase_S28_2nd	e3n0tB2	A: alpha arrays	X: Dipeptidyl-peptidase 2 helical domain (From Topology)	H: Dipeptidyl-peptidase 2 helical domain (From Topology)	T: Dipeptidyl-peptidase 2 helical domain	F: Peptidase_S28_2nd	ECOD (1.6)
B	Peptidase_S28_1st	e3n0tB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Peptidase_S28_1st	ECOD (1.6)
C	Peptidase_S28_2nd	e3n0tC2	A: alpha arrays	X: Dipeptidyl-peptidase 2 helical domain (From Topology)	H: Dipeptidyl-peptidase 2 helical domain (From Topology)	T: Dipeptidyl-peptidase 2 helical domain	F: Peptidase_S28_2nd	ECOD (1.6)
C	Peptidase_S28_1st	e3n0tC1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Peptidase_S28_1st	ECOD (1.6)
D	Peptidase_S28_2nd	e3n0tD2	A: alpha arrays	X: Dipeptidyl-peptidase 2 helical domain (From Topology)	H: Dipeptidyl-peptidase 2 helical domain (From Topology)	T: Dipeptidyl-peptidase 2 helical domain	F: Peptidase_S28_2nd	ECOD (1.6)
D	Peptidase_S28_1st	e3n0tD1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Peptidase_S28_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
A	1.20.120.980	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Serine carboxypeptidase S28, SKS domain	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	1.20.120.980	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Serine carboxypeptidase S28, SKS domain	CATH (4.3.0)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
C	1.20.120.980	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Serine carboxypeptidase S28, SKS domain	CATH (4.3.0)
D	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
D	1.20.120.980	Mainly Alpha	Up-down Bundle	Four Helix Bundle (Hemerythrin (Met), subunit A)	Serine carboxypeptidase S28, SKS domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF05577	Serine carboxypeptidase S28 (Peptidase_S28)	Serine carboxypeptidase S28	These serine proteases include several eukaryotic enzymes such as lysosomal Pro-X carboxypeptidase, dipeptidyl-peptidase II, and thymus-specific serine peptidase.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Dipeptidyl peptidase 2	peptidase activity catalytic activity, acting on a protein dipeptidyl-peptidase activity hydrolase activity exopeptidase activity catalytic activity serine-type exopeptidase activity serine hydrolase activity serine-type peptidase activity aminopeptidase activity	organonitrogen compound catabolic process organonitrogen compound metabolic process catabolic process protein catabolic process in the vacuole lysosomal protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process organic substance metabolic process metabolic process protein metabolic process macromolecule metabolic process organic substance catabolic process proteolysis	membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system vesicle extracellular region extracellular exosome extracellular vesicle extracellular organelle membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system vesicle extracellular region extracellular exosome extracellular vesicle extracellular organelle extracellular space extracellular membrane-bounded organelle lytic vacuole intracellular vesicle membrane-enclosed lumen cytoplasmic vesicle lumen vacuolar lumen intracellular organelle lumen cytoplasmic vesicle lysosome vesicle lumen azurophil granule vacuole secretory granule lumen azurophil granule lumen organelle lumen secretory granule primary lysosome secretory vesicle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR008758	Peptidase S28	Family
A, B, C, D	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B, C, D	IPR042269	Serine carboxypeptidase S28, SKS domain	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: Q9UHL4	Necrosis atypical teratoid rhabdoid tumor ovarian cancer medulloblastoma subependymal giant cell astrocytoma

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.