6EOS

DPP8 - Apo, space group 19

External Resource: Annotation

Domain Annotation: ECOD Classification
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)
F [auth B]	F_UNCLASSIFIED	e6eosB1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
F [auth B]	Hydrolase_4	e6eosB2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)
A	F_UNCLASSIFIED	e6eosA1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
A	Hydrolase_4	e6eosA2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)
B [auth C]	F_UNCLASSIFIED	e6eosC2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
B [auth C]	Hydrolase_4	e6eosC1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)
C [auth D]	F_UNCLASSIFIED	e6eosD1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
C [auth D]	Hydrolase_4	e6eosD2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)
D [auth E]	F_UNCLASSIFIED	e6eosE2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
D [auth E]	Hydrolase_4	e6eosE1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)
E [auth F]	F_UNCLASSIFIED	e6eosF1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
E [auth F]	Hydrolase_4	e6eosF2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	PF00930	Dipeptidyl peptidase IV (DPP IV) N-terminal region (DPPIV_N)	Dipeptidyl peptidase IV (DPP IV) N-terminal region	-	Repeat
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	PF00326	Prolyl oligopeptidase family (Peptidase_S9)	Prolyl oligopeptidase family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	Dipeptidyl peptidase 8	peptidase activity catalytic activity, acting on a protein dipeptidyl-peptidase activity hydrolase activity exopeptidase activity catalytic activity serine hydrolase activity serine-type peptidase activity aminopeptidase activity	response to stimulus immune response immune system process cellular process apoptotic process cell death programmed cell death proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process regulation of biological process regulation of cellular process response to stimulus immune response immune system process cellular process apoptotic process cell death programmed cell death proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process regulation of biological process regulation of cellular process negative regulation of programmed cell death biological regulation negative regulation of cellular process negative regulation of biological process regulation of programmed cell death	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	IPR045785	Dipeptidyl peptidase 8 /9 ,N-terminal	Domain
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	IPR050278	Serine protease S9B/DPPIV	Family
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	IPR001375	Peptidase S9, prolyl oligopeptidase, catalytic domain	Domain
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	IPR002469	Dipeptidylpeptidase IV, N-terminal domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B [auth C], C [auth D], D [auth E], E [auth F], A, B [auth C], C [auth D], D [auth E], E [auth F], F [auth B]	Pharos: Q6V1X1	atypical teratoid rhabdoid tumor lymphoplasmacytic lymphoma osteosarcoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia glioblastoma malignant glioma ovarian cancer plasma cell myeloma large cell medulloblastoma medulloblastoma pancreatic intraductal papillary-mucinous neoplasm type 2 diabetes mellitus

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.