5LLS

Porcine dipeptidyl peptidase IV in complex with 8-(3-aminopiperidin-1-yl)-7-[(2-bromophenyl)methyl]-1,3-dimethyl-2,3,6,7-tetrahydro-1H-purine-2,6-dione

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5llsa1	All beta proteins	8-bladed beta-propeller	DPP6 N-terminal domain-like	DPP6 N-terminal domain-like	automated matches	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
A	d5llsa2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
D	d5llsd1	All beta proteins	8-bladed beta-propeller	DPP6 N-terminal domain-like	DPP6 N-terminal domain-like	automated matches	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
D	d5llsd2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d5llsb1	All beta proteins	8-bladed beta-propeller	DPP6 N-terminal domain-like	DPP6 N-terminal domain-like	automated matches	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d5llsb2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
C	d5llsc1	All beta proteins	8-bladed beta-propeller	DPP6 N-terminal domain-like	DPP6 N-terminal domain-like	automated matches	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
C	d5llsc2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	DPPIV_N	e5llsA2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: DPPIV_N	ECOD (1.6)
A	Hydrolase_4	e5llsA3	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	DPPIV_N	e5llsD1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: DPPIV_N	ECOD (1.6)
D	Hydrolase_4	e5llsD2	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	DPPIV_N	e5llsB2	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: DPPIV_N	ECOD (1.6)
B	Hydrolase_4	e5llsB3	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	DPPIV_N	e5llsC1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 8-bladed	F: DPPIV_N	ECOD (1.6)
C	Hydrolase_4	e5llsC2	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)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.140.10.30	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	CATH (4.3.0)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
D	2.140.10.30	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	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)
B	2.140.10.30	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	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)
C	2.140.10.30	Mainly Beta	8 Propeller	Methanol Dehydrogenase	Chain A	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00930	Dipeptidyl peptidase IV (DPP IV) N-terminal region (DPPIV_N)	Dipeptidyl peptidase IV (DPP IV) N-terminal region	-	Repeat
A, B, C, D	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, C, D	Dipeptidyl peptidase 4	peptidase activity catalytic activity, acting on a protein dipeptidyl-peptidase activity hydrolase activity exopeptidase activity catalytic activity protein binding binding signaling receptor binding enzyme binding protease binding serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity peptidase activity catalytic activity, acting on a protein dipeptidyl-peptidase activity hydrolase activity exopeptidase activity catalytic activity protein binding binding signaling receptor binding enzyme binding protease binding serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity identical protein binding protein homodimerization activity protein dimerization activity aminopeptidase activity	endothelial cell migration cell migration cellular process cell motility regulation of biological process cell population proliferation regulation of cellular process positive regulation of cell population proliferation regulation of cell population proliferation biological regulation positive regulation of biological process positive regulation of cellular process cell adhesion cellular component disassembly endothelial cell migration cell migration cellular process cell motility regulation of biological process cell population proliferation regulation of cellular process positive regulation of cell population proliferation regulation of cell population proliferation biological regulation positive regulation of biological process positive regulation of cellular process cell adhesion cellular component disassembly negative regulation of extracellular matrix organization extracellular matrix disassembly regulation of cellular component organization negative regulation of cellular component organization negative regulation of biological process extracellular matrix organization cellular component organization negative regulation of extracellular matrix disassembly negative regulation of cellular process cellular component organization or biogenesis regulation of extracellular matrix organization regulation of extracellular matrix disassembly extracellular structure organization external encapsulating structure organization multicellular organismal process regulation of leukocyte activation regulation of cell activation positive regulation of leukocyte cell-cell adhesion lymphocyte activation leukocyte cell-cell adhesion leukocyte activation positive regulation of cell-cell adhesion positive regulation of lymphocyte activation positive regulation of cell activation cell-cell adhesion T cell activation positive regulation of leukocyte activation regulation of multicellular organismal process regulation of immune system process regulation of cell-cell adhesion positive regulation of immune system process positive regulation of T cell activation positive regulation of cell adhesion regulation of cell adhesion cell activation regulation of T cell activation immune system process lymphocyte costimulation regulation of leukocyte cell-cell adhesion positive regulation of multicellular organismal process T cell costimulation regulation of lymphocyte activation proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cell projection cellular anatomical structure cell leading edge plasma membrane bounded cell projection lamellipodium cell periphery apical part of cell membrane plasma membrane plasma membrane region apical plasma membrane cell surface anchoring junction cell junction cell projection cellular anatomical structure cell leading edge plasma membrane bounded cell projection lamellipodium cell periphery apical part of cell membrane plasma membrane plasma membrane region apical plasma membrane cell surface anchoring junction cell junction membrane microdomain membrane raft membrane-bounded organelle intracellular anatomical structure intracellular vesicle intracellular membrane-bounded organelle intracellular organelle cytoplasmic vesicle organelle cytoplasm vesicle endocytic vesicle leading edge membrane lamellipodium membrane cell projection membrane extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001375	Peptidase S9, prolyl oligopeptidase, catalytic domain	Domain
A, B, C, D	IPR040522	Dipeptidyl peptidase 4, low complexity region	Domain
A, B, C, D	IPR050278	Serine protease S9B/DPPIV	Family
A, B, C, D	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B, C, D	IPR002471	Peptidase S9, serine active site	Active Site
A, B, C, D	IPR002469	Dipeptidylpeptidase IV, N-terminal domain	Domain

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.