Annotations: 6NFF

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF08531	e6nffA1	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF08531	ECOD (1.6)
A	PF09168	e6nffA3	A: alpha bundles	X: CH domain-like	H: X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain (From Topology)	T: X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain	F: PF09168	ECOD (1.6)
A	PF02129	e6nffA2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF02129	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 (utative)
A	1.10.246.70	Mainly Alpha	Orthogonal Bundle	Serum Albumin	Chain A, Domain 1	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09168	X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal (PepX_N)	X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal	Members of this family adopt a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N-terminus also form ...	Members of this family adopt a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N-terminus also forms a small parallel beta sheet with strand 5' of catalytic domain. The domain mediates dimerisation of the protein, with two proline residues present in the domain being critical for interaction [1].	Domain
A	PF08530	X-Pro dipeptidyl-peptidase C-terminal non-catalytic domain (PepX_C)	X-Pro dipeptidyl-peptidase C-terminal non-catalytic domain	This domain contains a beta sandwich domain.	Domain
A	PF02129	X-Pro dipeptidyl-peptidase (S15 family) (Peptidase_S15)	X-Pro dipeptidyl-peptidase (S15 family)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Xaa-Pro dipeptidyl-peptidase	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	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036313	PepX, N-terminal domain superfamily	Homologous Superfamily
A	IPR000383	Xaa-Pro dipeptidyl-peptidase-like domain	Domain
A	IPR013736	Xaa-Pro dipeptidyl-peptidase, C-terminal	Domain
A	IPR008252	Peptidase S15, X-Pro dipeptidyl-peptidase	Family
A	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A	IPR015251	X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal domain	Domain
A	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A	IPR005674	CocE/Serine esterase	Family

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 R01GM133198.