7ZXS

Crystal structure of DPP9 in complex with a 4-oxo-b-lactam based inhibitor, A295

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	F_UNCLASSIFIED	e7zxsB2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
B	Hydrolase_4	e7zxsB1	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	F_UNCLASSIFIED	e7zxsD2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
D	Hydrolase_4	e7zxsD1	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	e7zxsA1	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	e7zxsA2	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	F_UNCLASSIFIED	e7zxsC1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: F_UNCLASSIFIED	ECOD (1.6)
C	Hydrolase_4	e7zxsC2	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
B, D	PF00930	Dipeptidyl peptidase IV (DPP IV) N-terminal region (DPPIV_N)	Dipeptidyl peptidase IV (DPP IV) N-terminal region	-	Repeat
B, D	PF00326	Prolyl oligopeptidase family (Peptidase_S9)	Prolyl oligopeptidase family	-	Domain
B, D	PF19520	Dipeptidyl peptidase 8 and 9 N-terminal (Dpp_8_9_N)	Dipeptidyl peptidase 8 and 9 N-terminal	-	Repeat
A, C	PF00930	Dipeptidyl peptidase IV (DPP IV) N-terminal region (DPPIV_N)	Dipeptidyl peptidase IV (DPP IV) N-terminal region	-	Repeat
A, C	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
B, D	Dipeptidyl peptidase 9	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 identical protein binding protein binding binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process response to stimulus defense response response to stress pyroptotic inflammatory response inflammatory response regulation of biological process regulation of cellular process negative regulation of programmed cell death proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process response to stimulus defense response response to stress pyroptotic inflammatory response inflammatory response 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 cell death programmed cell death	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell leading edge polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell leading edge polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer supramolecular complex microtubule cytoskeleton membrane-bounded organelle nucleus intracellular membrane-bounded organelle
A, C	Dipeptidyl peptidase 9	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 identical protein binding protein binding binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process response to stimulus defense response response to stress pyroptotic inflammatory response inflammatory response regulation of biological process regulation of cellular process negative regulation of programmed cell death proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process response to stimulus defense response response to stress pyroptotic inflammatory response inflammatory response 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 cell death programmed cell death	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell leading edge polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell leading edge polymeric cytoskeletal fiber intracellular membraneless organelle intracellular organelle cytoskeleton organelle membraneless organelle supramolecular fiber microtubule supramolecular polymer supramolecular complex microtubule cytoskeleton membrane-bounded organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

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

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
B, D	Pharos: Q86TI2	idiopathic pulmonary fibrosis acute interstitial pneumonia idiopathic interstitial pneumonia Sjogren syndrome diabetes mellitus type 2 diabetes mellitus Hamman-Rich syndrome polycystic ovary syndrome
A, C	Pharos: Q86TI2	idiopathic pulmonary fibrosis acute interstitial pneumonia idiopathic interstitial pneumonia Sjogren syndrome diabetes mellitus type 2 diabetes mellitus Hamman-Rich syndrome polycystic ovary syndrome

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, C	CSO	Parent Component: CYS RESID: AA0205 PSI-MOD : L-cysteine sulfenic acid MOD:00210

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.