5JBQ

EF-TU (ESCHERICHIA COLI) IN COMPLEX WITH THIOMURACIN ANALOG

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation
Structure Motif: Primary M-CSA Annotation

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	8056349	3002022	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	EF-Tu post-G domain-like	8056352	3002024	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	EF-Tu post-G domain-like	8056350	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	PF03144	e5jbqA2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: PF03144	ECOD (1.6)
A	PF03143	e5jbqA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Aminomethyltransferase beta-barrel domain	F: PF03143	ECOD (1.6)
A	PF00009	e5jbqA3	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)

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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
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	PF03143	Elongation factor Tu C-terminal domain (GTP_EFTU_D3)	Elongation factor Tu C-terminal domain	Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA [1] and binding to EF-Ts Pfam:PF00889 [2].	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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Elongation factor Tu 1	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 regulator activity translation regulator activity, nucleic acid binding translation elongation factor activity nucleic acid binding translation factor activity, RNA binding RNA 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	response to stimulus response to chemical response to antibiotic 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 translational elongation response to stimulus response to chemical response to antibiotic 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 translational elongation organic substance biosynthetic process metabolic process cellular process macromolecule metabolic process protein metabolic process	cell periphery plasma membrane membrane cellular anatomical entity intracellular anatomical structure cytoplasm protein-containing complex guanyl-nucleotide exchange factor complex intracellular protein-containing complex
B	THIOMURACIN ANALOG	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000795	Translational (tr)-type GTP-binding domain	Domain
A	IPR033720	Elongation factor Tu, domain 2	Domain
A	IPR009001	Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal	Homologous Superfamily
A	IPR031157	Tr-type G domain, conserved site	Conserved Site
A	IPR004541	Translation elongation factor EFTu/EF1A, bacterial/organelle	Family
A	IPR004161	Translation elongation factor EFTu-like, domain 2	Domain
A	IPR009000	Translation protein, beta-barrel domain superfamily	Homologous Superfamily
A	IPR004160	Translation elongation factor EFTu/EF1A, C-terminal	Domain
A	IPR005225	Small GTP-binding protein domain	Domain
A	IPR041709	Elongation factor Tu (EF-Tu), GTP-binding domain	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B	05N	Parent Component: PRO
B	6RK
B	BB6	Parent Component: CYS
B	BB9	Parent Component: CYS RESID: AA0241 , AA0242 , AA0243 , AA0244 , AA0466 , AA0467 , AA0485 , AA0541 PSI-MOD : glycine thiazole-4-carboxylic acid MOD:00246 , L-serine thiazole-4-carboxylic acid MOD:00247 , L-phenylalanine thiazole-4-carboxylic acid MOD:00248 , L-cysteine thiazole-4-carboxylic acid MOD:00249 , L-isoleucine thiazole-4-carboxylic acid MOD:01389 , L-valine thiazole-4-carboxylic acid MOD:01390 , L-threonine thiazoline-4-carboxylic acid MOD:01408 , L-glutamate thiazole-4-carboxylic acid MOD:01815
B	H14	Parent Component: PHE RESID: AA0241 , AA0242 , AA0243 , AA0244 , AA0466 , AA0467 , AA0485 , AA0541
B	MH6	Parent Component: SER RESID: AA0241 , AA0242 , AA0243 , AA0244 , AA0466 , AA0467 , AA0485 , AA0541 , AA0540 PSI-MOD : glycine thiazole-4-carboxylic acid MOD:00246 , L-serine thiazole-4-carboxylic acid MOD:00247 , L-phenylalanine thiazole-4-carboxylic acid MOD:00248 , L-cysteine thiazole-4-carboxylic acid MOD:00249 , L-isoleucine thiazole-4-carboxylic acid MOD:01389 , L-valine thiazole-4-carboxylic acid MOD:01390 , L-threonine thiazoline-4-carboxylic acid MOD:01408 , L-glutamate thiazole-4-carboxylic acid MOD:01815 , L-cysteine 3-hydroxy-2,5-pyridinedicarboxylic acid MOD:01814

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	protein-synthesizing GTPase (elongation factor Tu) M-CSA #535	Elongation factor Tu hydrolyses GTP to give GDP and Pi, thus providing the free energy that the ribosome needs to incorporate amino acids into the growing polypeptide. As such, it shows homology to other GTP binding proteins such as the oncogene ras, but may show a different mechanism of GTP hydrolysis. Many antibiotics are able to inhibit EFTu, making study of its mechanism particularly useful in view of the possibility of synthesising new antibiotics.	Defined by 1 residue: GLY:A-84 [auth A-83] \| Explore in 3D: M-CSA Motif Definition At least 2 residues must be present to support Structure Motif searching.

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.