Annotations: 1FNM

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1fnma1	All beta proteins	Reductase/isomerase/elongation factor common domain	Translation proteins	Elongation factors	Elongation factor G (EF-G), domain II	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
A	d1fnma2	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	G proteins	Elongation factor G (EF-G), N-terminal (G) domain	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
A	d1fnma3	Alpha and beta proteins (a+b)	Ribosomal protein S5 domain 2-like	Ribosomal protein S5 domain 2-like	Translational machinery components	Elongation factor G (EF-G), domain IV	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
A	d1fnma4	Alpha and beta proteins (a+b)	Ferredoxin-like	EF-G C-terminal domain-like	EF-G/eEF-2 domains III and V	Elongation factor G (EF-G)	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ras-like P-loop GTPases	8038316	3002022	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	EF-G C-terminal domain-like	8038318	3001287	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	EF-G C-terminal domain-like	8038320	3001287	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Ribosomal protein S5 domain 2-like	8038317	3000100	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	EF-Tu post-G domain-like	8038315	3002024	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	GTP_EFTU_D2	e1fnmA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: GTP_EFTU_D2	ECOD (1.6)
A	EFG_IV	e1fnmA4	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: EFG_IV	ECOD (1.6)
A	EFG_C	e1fnmA3	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: EFG_C	ECOD (1.6)
A	EFG_II	e1fnmA2	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: EFG_II	ECOD (1.6)
A	MnmE_helical_2nd	e1fnmA5	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)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)
A	2.40.30.10	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
A	3.30.70.870	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Elongation Factor G (Translational Gtpase), domain 3	CATH (4.3.0)
A	3.30.230.10	Alpha Beta	2-Layer Sandwich	Ribosomal Protein S5	domain 2	CATH (4.3.0)
A	3.30.70.240	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00679	Elongation factor G C-terminus (EFG_C)	Elongation factor G C-terminus	This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.	Domain
A	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	PF14492	Elongation Factor G, domain III (EFG_III)	Elongation Factor G, domain III	This domain is found in Elongation Factor G. It shares a similar structure with domain V (Pfam:PF00679). Structural studies in drosophila indicate this is domain 3 [1].	Domain
A	PF03144	Elongation factor Tu domain 2 (GTP_EFTU_D2)	Elongation factor Tu domain 2	Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as e ...	Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to Pfam:PF03143, and in fact has weak sequence matches to this domain.	Domain
A	PF03764	Elongation factor G, domain IV (EFG_IV)	Elongation factor G, domain IV	This domain is found in elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopts a ribosomal protein S5 domain 2-like fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ELONGATION FACTOR G	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding guanyl nucleotide binding nucleotide binding GDP binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding guanyl nucleotide binding nucleotide binding GDP binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding translation regulator activity translation regulator activity, nucleic acid binding translation elongation factor activity nucleic acid binding translation factor activity, RNA binding ribonucleoprotein complex binding protein-containing complex binding ribosome binding 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	biosynthetic process translational elongation metabolic process cellular process primary metabolic process macromolecule metabolic process protein metabolic process translation gene expression macromolecule biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR005225	Small GTP-binding domain	Domain
A	IPR005517	Translation elongation factor EFG/EF2, domain IV	Domain
A	IPR004540	Translation elongation factor EFG/EF2	Family
A	IPR000795	Translational (tr)-type GTP-binding domain	Domain
A	IPR000640	Elongation factor EFG, domain V-like	Domain
A	IPR031157	Tr-type G domain, conserved site	Conserved Site
A	IPR009022	Elongation factor G, domain III	Domain
A	IPR035647	EF-G domain III/V-like	Homologous Superfamily
A	IPR041095	Elongation Factor G, domain II	Domain
A	IPR004161	Translation elongation factor EFTu-like, domain 2	Domain
A	IPR047872	Elongation factor G, domain IV	Domain
A	IPR009000	Translation protein, beta-barrel domain superfamily	Homologous Superfamily
A	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A	IPR035649	EFG, domain V	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A	IPR014721	Small ribosomal subunit protein uS5 domain 2-type fold, subgroup	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.