Annotations: 3TR5

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
D	SCOP2B Superfamily	Ras-like P-loop GTPases	8092481	3002022	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	EF-Tu post-G domain-like	8092482	3002024	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	EF-G C-terminal domain-like	8092479	3001287	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	EF-G C-terminal domain-like	8092480	3001287	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Ras-like P-loop GTPases	8092481	3002022	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	EF-G C-terminal domain-like	8092479	3001287	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	EF-Tu post-G domain-like	8092482	3002024	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	EF-G C-terminal domain-like	8092480	3001287	SCOP2B (2022-06-29)
B	SCOP2 Family	RF3 C-terminal domain-like	8045934	4004772	SCOP2 (2022-06-29)
B	SCOP2 Family	Translation factor common region-like	8092478	4004050	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	EF-G C-terminal domain-like	8092479	3001287	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Ras-like P-loop GTPases	8092481	3002022	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	EF-G C-terminal domain-like	8092480	3001287	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	EF-Tu post-G domain-like	8092482	3002024	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	EF-G C-terminal domain-like	8092479	3001287	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	EF-G C-terminal domain-like	8092480	3001287	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	EF-Tu post-G domain-like	8092482	3002024	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Ras-like P-loop GTPases	8092481	3002022	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	GTP_EFTU_D2	e3tr5D15	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2	ECOD (1.6)
D	UNK_F_TYPE	e3tr5D14	A: a+b two layers	X: Alpha-beta plaits	H: EF-G C-terminal domain-like (From Topology)	T: EF-G C-terminal domain-like	F: UNK_F_TYPE	ECOD (1.6)
D	MnmE_helical_2nd	e3tr5D13	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: MnmE_helical_2nd	ECOD (1.6)
A	GTP_EFTU_D2	e3tr5A9	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2	ECOD (1.6)
A	UNK_F_TYPE	e3tr5A8	A: a+b two layers	X: Alpha-beta plaits	H: EF-G C-terminal domain-like (From Topology)	T: EF-G C-terminal domain-like	F: UNK_F_TYPE	ECOD (1.6)
A	MnmE_helical_2nd	e3tr5A7	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: MnmE_helical_2nd	ECOD (1.6)
B	GTP_EFTU_D2	e3tr5B6	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2	ECOD (1.6)
B	UNK_F_TYPE	e3tr5B5	A: a+b two layers	X: Alpha-beta plaits	H: EF-G C-terminal domain-like (From Topology)	T: EF-G C-terminal domain-like	F: UNK_F_TYPE	ECOD (1.6)
B	MnmE_helical_2nd	e3tr5B4	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: MnmE_helical_2nd	ECOD (1.6)
C	GTP_EFTU_D2	e3tr5C15	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2	ECOD (1.6)
C	UNK_F_TYPE	e3tr5C14	A: a+b two layers	X: Alpha-beta plaits	H: EF-G C-terminal domain-like (From Topology)	T: EF-G C-terminal domain-like	F: UNK_F_TYPE	ECOD (1.6)
C	MnmE_helical_2nd	e3tr5C13	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: MnmE_helical_2nd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
D	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
D	3.30.70.3280	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Peptide chain release factor 3, domain III	CATH (4.3.0)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
A	3.30.70.3280	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Peptide chain release factor 3, domain III	CATH (4.3.0)
B	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
B	3.30.70.3280	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Peptide chain release factor 3, domain III	CATH (4.3.0)
C	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
C	3.30.70.3280	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Peptide chain release factor 3, domain III	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00009	Elongation factor Tu GTP binding domain (GTP_EFTU)	Elongation factor Tu GTP binding domain	This domain contains a P-loop motif, also found in several other families such as Pfam:PF00071, Pfam:PF00025 and Pfam:PF00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.	Domain
A, B, C, D	PF22042	Elongation factor G domain 2 (EF-G_D2)	Elongation factor G domain 2	Elongation factor G (EF-G) catalyzes the translocation step of translation. It consists of five structural domains, this entry represents the second domain [1]. This domain adopts a beta barrel structure. This family also includes domains found in ot ...	Elongation factor G (EF-G) catalyzes the translocation step of translation. It consists of five structural domains, this entry represents the second domain [1]. This domain adopts a beta barrel structure. This family also includes domains found in other translation factors such as translation initiation factor IF-2, peptide chain release factor, etc.	Domain
A, B, C, D	PF16658	Class II release factor RF3, C-terminal domain (RF3_C)	Class II release factor RF3, C-terminal domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Peptide chain release factor 3	guanosine tetraphosphate binding guanyl nucleotide binding binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding guanosine tetraphosphate binding guanyl nucleotide binding binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding translation release factor activity, codon specific translation regulator activity translation regulator activity, nucleic acid binding translation release factor activity nucleic acid binding translation termination factor activity translation factor activity, RNA binding translation release factor activity, codon nonspecific GTP binding purine ribonucleoside triphosphate binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	cellular component disassembly protein-containing complex organization protein-containing complex disassembly primary metabolic process translation gene expression macromolecule biosynthetic process cellular component organization biosynthetic process cellular process metabolic process translational termination cellular component organization or biogenesis protein metabolic process cellular component disassembly protein-containing complex organization protein-containing complex disassembly primary metabolic process translation gene expression macromolecule biosynthetic process cellular component organization biosynthetic process cellular process metabolic process translational termination cellular component organization or biogenesis protein metabolic process macromolecule metabolic process regulation of cellular process regulation of cellular component organization regulation of protein-containing complex disassembly regulation of primary metabolic process post-transcriptional regulation of gene expression regulation of biosynthetic process regulation of biological process regulation of protein metabolic process regulation of translational termination biological regulation regulation of macromolecule metabolic process regulation of gene expression regulation of translation regulation of macromolecule biosynthetic process regulation of metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR005225	Small GTP-binding domain	Domain
A, B, C, D	IPR032090	Peptide chain release factor 3, C-terminal	Domain
A, B, C, D	IPR000795	Translational (tr)-type GTP-binding domain	Domain
A, B, C, D	IPR041732	Peptide chain release factor 3, GTP-binding domain	Domain
A, B, C, D	IPR031157	Tr-type G domain, conserved site	Conserved Site
A, B, C, D	IPR035647	EF-G domain III/V-like	Homologous Superfamily
A, B, C, D	IPR053905	Elongation factor G-like, domain II	Domain
A, B, C, D	IPR004548	Peptide chain release factor 3	Family
A, B, C, D	IPR009000	Translation protein, beta-barrel domain superfamily	Homologous Superfamily
A, B, C, D	IPR038467	Peptide chain release factor 3, domain III superfamily	Homologous Superfamily
A, B, C, D	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

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.