3ZZS

Engineered 12-subunit Bacillus stearothermophilus trp RNA-binding attenuation protein (TRAP)

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)
A	d3zzsa_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
D	d3zzsd_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
E	d3zzse_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
F	d3zzsf_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
G	d3zzsg_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
H	d3zzsh_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
I	d3zzsi_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
B	d3zzsb_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)
C	d3zzsc_	All beta proteins	Double-stranded beta-helix	TRAP-like	Trp RNA-binding attenuation protein (TRAP)	automated matches	(Geobacillus stearothermophilus ) [TaxId: 1422 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	TRAP-like	8038933	3001865	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	TRAP-like	8038933	3001865	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	TRAP-like	8038933	3001865	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	TRAP-like	8038933	3001865	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	TRAP-like	8038933	3001865	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	TRAP-like	8038933	3001865	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	TRAP-like	8038933	3001865	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	TRAP-like	8038933	3001865	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	TRAP-like	8038933	3001865	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)
A	TrpBP	e3zzsA1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)
D	TrpBP	e3zzsD1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)
E	TrpBP	e3zzsE1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)
F	TrpBP	e3zzsF1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)
G	TrpBP	e3zzsG1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)
H	TrpBP	e3zzsH1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)
I	TrpBP	e3zzsI1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)
B	TrpBP	e3zzsB1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)
C	TrpBP	e3zzsC1	A: beta sandwiches	X: jelly-roll	H: Trp RNA-binding attenuation protein (TRAP) (From Topology)	T: Trp RNA-binding attenuation protein (TRAP)	F: TrpBP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	CATH (4.3.0)
D	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	CATH (4.3.0)
E	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	CATH (4.3.0)
F	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	CATH (4.3.0)
G	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	CATH (4.3.0)
H	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	CATH (4.3.0)
I	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	CATH (4.3.0)
B	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	CATH (4.3.0)
C	2.60.40.50	Mainly Beta	Sandwich	Immunoglobulin-like	TRAP-like	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, G, H, I	PF02081	Tryptophan RNA-binding attenuator protein (TrpBP)	Tryptophan RNA-binding attenuator protein	-	Domain

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, G, H, I	TRANSCRIPTION ATTENUATION PROTEIN MTRB	RNA binding binding organic cyclic compound binding nucleic acid binding identical protein binding protein binding	RNA metabolic process primary metabolic process nucleobase-containing compound biosynthetic process gene expression DNA-templated transcription termination macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process biosynthetic process metabolic process cellular process RNA metabolic process primary metabolic process nucleobase-containing compound biosynthetic process gene expression DNA-templated transcription termination macromolecule biosynthetic process nucleic acid metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process biosynthetic process metabolic process cellular process macromolecule metabolic process regulation of cellular process regulation of primary metabolic process regulation of RNA metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of biological process biological regulation regulation of macromolecule metabolic process regulation of gene expression regulation of macromolecule biosynthetic process regulation of DNA-templated transcription regulation of metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR016031	Tryptophan RNA-binding attenuator protein-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR000824	Transcription attenuation protein MtrB	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I	IPR023558	Tryptophan RNA-binding attenuator protein 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.