Annotations: 1ZO1

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C [auth W]	d1zo1w1	All beta proteins	OB-fold	Nucleic acid-binding proteins	Cold shock DNA-binding domain-like	Translational initiation factor 1, IF1	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C [auth W]	SCOP2B Superfamily	Nucleic acid-binding proteins	8086090	3000135	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)
B [auth I]	PF03144	e1zo1I8	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: PF03144	ECOD (1.6)
B [auth I]	PF22042	e1zo1I9	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: PF22042	ECOD (1.6)
B [auth I]	PF00009	e1zo1I1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00009	ECOD (1.6)
B [auth I]	PF11987	e1zo1I10	A: a/b three-layered sandwiches	X: Initiation factor IF2/eIF5b, domain 3 (From Topology)	H: Initiation factor IF2/eIF5b, domain 3 (From Topology)	T: Initiation factor IF2/eIF5b, domain 3	F: PF11987	ECOD (1.6)
C [auth W]	PF01176	e1zo1W1	A: beta barrels	X: OB-fold	H: Nucleic acid-binding proteins (From Topology)	T: Nucleic acid-binding proteins	F: PF01176	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B [auth I]	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
B [auth I]	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
B [auth I]	PF11987	Translation-initiation factor 2 (IF-2)	Translation-initiation factor 2	IF-2 is a translation initiator in each of the three main phylogenetic domains (Eukaryotes [1], Bacteria [2] and Archaea [3]). IF2 interacts with formylmethionine-tRNA, GTP, IF1, IF3 and both ribosomal subunits [2]. Through these interactions, IF2 pr ...	IF-2 is a translation initiator in each of the three main phylogenetic domains (Eukaryotes [1], Bacteria [2] and Archaea [3]). IF2 interacts with formylmethionine-tRNA, GTP, IF1, IF3 and both ribosomal subunits [2]. Through these interactions, IF2 promotes the binding of the initiator tRNA to the A site in the smaller ribosomal subunit and catalyses the hydrolysis of GTP following initiation-complex formation [2].	Domain
C [auth W]	PF01176	Translation initiation factor 1A / IF-1 (eIF-1a)	Translation initiation factor 1A / IF-1	This family includes both the eukaryotic translation factor eIF-1A and the bacterial translation initiation factor IF-1.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth F]	P/I-site tRNA	-	-	-
B [auth I]	translation initiation factor 2	translation regulator activity binding organic cyclic compound binding translation regulator activity, nucleic acid binding nucleic acid binding translation initiation factor activity translation factor activity, RNA binding guanosine tetraphosphate binding guanyl nucleotide binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding translation regulator activity binding organic cyclic compound binding translation regulator activity, nucleic acid binding nucleic acid binding translation initiation factor activity translation factor activity, RNA binding guanosine tetraphosphate binding guanyl nucleotide binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule 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 ribonucleoprotein complex binding protein-containing complex binding ribosomal small subunit binding ribosome binding	organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process primary metabolic process translation gene expression macromolecule biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process translational initiation metabolic process cellular process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process primary metabolic process translation gene expression macromolecule biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process translational initiation metabolic process cellular process protein metabolic process macromolecule metabolic process response to stimulus response to stress response to abiotic stimulus response to cold response to temperature stimulus chaperone-mediated protein folding protein maturation protein folding	membrane cellular anatomical entity intracellular anatomical structure cytoplasm cytosol
C [auth W]	translation Initiation Factor 1	translation regulator activity binding organic cyclic compound binding translation regulator activity, nucleic acid binding nucleic acid binding translation initiation factor activity translation factor activity, RNA binding RNA binding rRNA binding ribonucleoprotein complex binding protein-containing complex binding ribosome binding	-	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B [auth I]	IPR009061	Putative DNA-binding domain superfamily	Homologous Superfamily
B [auth I]	IPR000178	Translation initiation factor IF-2, bacterial-like	Family
B [auth I]	IPR000795	Translational (tr)-type GTP-binding domain	Domain
B [auth I]	IPR013575	Initiation factor 2 associated domain, bacterial	Domain
B [auth I]	IPR004161	Translation elongation factor EFTu-like, domain 2	Domain
B [auth I]	IPR006847	Translation initiation factor IF-2, N-terminal	Domain
B [auth I]	IPR044145	Translation initiation factor IF-2, domain II	Domain
B [auth I]	IPR009000	Translation protein, beta-barrel domain superfamily	Homologous Superfamily
B [auth I]	IPR005225	Small GTP-binding protein domain	Domain
B [auth I]	IPR015760	Translation initiation factor IF- 2	Family
B [auth I]	IPR036925	Translation initiation factor IF-2, domain 3 superfamily	Homologous Superfamily
B [auth I]	IPR023115	Translation initiation factor IF- 2, domain 3	Domain
B [auth I]	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
C [auth W]	IPR003029	S1 domain	Domain
C [auth W]	IPR012340	Nucleic acid-binding, OB-fold	Homologous Superfamily
C [auth W]	IPR006196	RNA-binding domain, S1, IF1 type	Domain
C [auth W]	IPR004368	Translation initiation factor IF-1	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.