6AQ3

Crystal structure of a trafficking protein particle complex subunit 3 from Naegleria fowleri covalently bound to palmitic acid

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 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)
D	d6aq3d_	Alpha and beta proteins (a+b)	Ligand-binding domain in the NO signalling and Golgi transport	Ligand-binding domain in the NO signalling and Golgi transport	automated matches	automated matches	(Naegleria fowleri ) [TaxId: 5763 ],	SCOPe (2.08)
A	d6aq3a_	Alpha and beta proteins (a+b)	Ligand-binding domain in the NO signalling and Golgi transport	Ligand-binding domain in the NO signalling and Golgi transport	automated matches	automated matches	(Naegleria fowleri ) [TaxId: 5763 ],	SCOPe (2.08)
B	d6aq3b_	Alpha and beta proteins (a+b)	Ligand-binding domain in the NO signalling and Golgi transport	Ligand-binding domain in the NO signalling and Golgi transport	automated matches	automated matches	(Naegleria fowleri ) [TaxId: 5763 ],	SCOPe (2.08)
C	d6aq3c_	Alpha and beta proteins (a+b)	Ligand-binding domain in the NO signalling and Golgi transport	Ligand-binding domain in the NO signalling and Golgi transport	automated matches	automated matches	(Naegleria fowleri ) [TaxId: 5763 ],	SCOPe (2.08)
E	d6aq3e_	Alpha and beta proteins (a+b)	Ligand-binding domain in the NO signalling and Golgi transport	Ligand-binding domain in the NO signalling and Golgi transport	automated matches	automated matches	(Naegleria fowleri ) [TaxId: 5763 ],	SCOPe (2.08)
F	d6aq3f_	Alpha and beta proteins (a+b)	Ligand-binding domain in the NO signalling and Golgi transport	Ligand-binding domain in the NO signalling and Golgi transport	automated matches	automated matches	(Naegleria fowleri ) [TaxId: 5763 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
D	SCOP2B Superfamily	Ligand-binding domain in the NO signalling and Golgi transport	8095321	3001668	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Ligand-binding domain in the NO signalling and Golgi transport	8095321	3001668	SCOP2B (2022-06-29)
B	SCOP2 Family	TRAPP components	8095320	4003802	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Ligand-binding domain in the NO signalling and Golgi transport	8095321	3001668	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Ligand-binding domain in the NO signalling and Golgi transport	8095321	3001668	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Ligand-binding domain in the NO signalling and Golgi transport	8095321	3001668	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Ligand-binding domain in the NO signalling and Golgi transport	8095321	3001668	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
D	PF04051	e6aq3D1	A: a+b complex topology	X: H-NOX domain (From Topology)	H: H-NOX domain (From Topology)	T: H-NOX domain	F: PF04051	ECOD (1.6)
A	PF04051	e6aq3A1	A: a+b complex topology	X: H-NOX domain (From Topology)	H: H-NOX domain (From Topology)	T: H-NOX domain	F: PF04051	ECOD (1.6)
B	PF04051	e6aq3B1	A: a+b complex topology	X: H-NOX domain (From Topology)	H: H-NOX domain (From Topology)	T: H-NOX domain	F: PF04051	ECOD (1.6)
C	PF04051	e6aq3C1	A: a+b complex topology	X: H-NOX domain (From Topology)	H: H-NOX domain (From Topology)	T: H-NOX domain	F: PF04051	ECOD (1.6)
E	PF04051	e6aq3E1	A: a+b complex topology	X: H-NOX domain (From Topology)	H: H-NOX domain (From Topology)	T: H-NOX domain	F: PF04051	ECOD (1.6)
F	PF04051	e6aq3F1	A: a+b complex topology	X: H-NOX domain (From Topology)	H: H-NOX domain (From Topology)	T: H-NOX domain	F: PF04051	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
D	3.30.1380.20	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)
A	3.30.1380.20	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)
B	3.30.1380.20	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)
C	3.30.1380.20	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)
E	3.30.1380.20	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)
F	3.30.1380.20	Alpha Beta	2-Layer Sandwich	Muramoyl-pentapeptide Carboxypeptidase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF04051	Transport protein particle (TRAPP) component (TRAPP)	Transport protein particle (TRAPP) component	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	trafficking protein particle complex subunit 3	-	localization transport cellular process establishment of localization Golgi vesicle transport vesicle-mediated transport	protein-containing complex intracellular protein-containing complex TRAPP complex vesicle tethering complex membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR024096	NO signalling/Golgi transport ligand-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR016721	Bet3 family	Family
A, B, C, D, E A, B, C, D, E, F	IPR007194	Transport protein particle (TRAPP) component	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.