1H3N

Leucyl-tRNA synthetase from Thermus thermophilus complexed with a sulphamoyl analogue of leucyl-adenylate

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	d1h3na1	All alpha proteins	Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases	Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases	Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases	Leucyl-tRNA synthetase (LeuRS)	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
A	d1h3na2	All beta proteins	ValRS/IleRS/LeuRS editing domain	ValRS/IleRS/LeuRS editing domain	ValRS/IleRS/LeuRS editing domain	Leucyl-tRNA synthetase (LeuRS)	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
A	d1h3na3	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	Class I aminoacyl-tRNA synthetases (RS), catalytic domain	Leucyl-tRNA synthetase (LeuRS)	(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	SCOP2 Family	Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases	8030025	4000856	SCOP2 (2022-06-29)
A	SCOP2 Family	ValRS/IleRS/LeuRS editing domain	8030026	4002332	SCOP2 (2022-06-29)
A	SCOP2 Family	Class I aminoacyl-tRNA synthetases (RS), catalytic domain	8030027	4003807	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases	8042404	3001786	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ValRS/IleRS/LeuRS editing domain	8042405	3001115	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Nucleotidylyl transferase	8042406	3001541	SCOP2 (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	tRNA-synt_1_2	e1h3nA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: acid protease	F: tRNA-synt_1_2	ECOD (1.6)
A	Anticodon_1,tRNA-synt_1g	e1h3nA2	A: alpha bundles	X: Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases (From Topology)	H: Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases (From Topology)	T: Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases	F: Anticodon_1,tRNA-synt_1g	ECOD (1.6)
A	tRNA-synt_1_1st	e1h3nA3	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: tRNA-synt_1_1st	ECOD (1.6)
A	tRNA-synt_1_3rd	e1h3nA4	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-related	T: Rubredoxin-related	F: tRNA-synt_1_3rd	ECOD (1.6)
A	tRNA-synt_1g	e1h3nA5	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-related	T: Rubredoxin-related	F: tRNA-synt_1g	ECOD (1.6)
A	UNK_F_TYPE	e1h3nA6	A: few secondary structure elements	X: Rubredoxin-like	H: Rubredoxin-like domain in leucyl-tRNA synthetase (LS2) (From Topology)	T: Rubredoxin-like domain in leucyl-tRNA synthetase (LS2)	F: UNK_F_TYPE	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	3.90.740.10	Alpha Beta	Alpha-Beta Complex	Isoleucyl-tRNA Synthetase	domain 2	CATH (4.3.0)
A	2.30.210.10	Mainly Beta	Roll	Leucyl-tRNA synthetase, domain 3	Leucyl-tRNA synthetase, domain 3	CATH (4.3.0)
A	1.10.730.10	Mainly Alpha	Orthogonal Bundle	Isoleucyl-tRNA Synthetase	Domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF13603	Leucyl-tRNA synthetase, editing domain (tRNA-synt_1_2)	Leucyl-tRNA synthetase, editing domain	This entry represents the editing domain in Leucine-tRNA ligase or Leucyl-tRNA synthetase, EC:6.1.1.4.	Domain
A	PF09334	tRNA synthetases class I (M) (tRNA-synt_1g)	tRNA synthetases class I (M)	-	Family
A	PF08264	Anticodon-binding domain of tRNA ligase (Anticodon_1)	Anticodon-binding domain of tRNA ligase	This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase.	Domain
A	PF14795	Leucine-tRNA synthetase-specific domain (Leucyl-specific)	Leucine-tRNA synthetase-specific domain	This short region is found only in leucyl-tRNA synthetases. It is flexibly linked to the enzyme-core by beta-ribbons structures [1]	Domain
A	PF00133	tRNA synthetases class I (I, L, M and V) (tRNA-synt_1)	tRNA synthetases class I (I, L, M and V)	Other tRNA synthetase sub-families are too dissimilar to be included.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	LEUCYL-TRNA SYNTHETASE	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding ligase activity, forming carbon-oxygen bonds aminoacyl-tRNA ligase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid leucine-tRNA ligase activity catalytic activity, acting on a tRNA catalytic activity ligase activity hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity aminoacyl-tRNA editing activity hydrolase activity cation binding metal ion binding	amino acid activation tRNA aminoacylation RNA metabolic process primary metabolic process amino acid metabolic process translation gene expression tRNA aminoacylation for protein translation macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process nucleobase-containing compound metabolic process biosynthetic process metabolic process amino acid activation tRNA aminoacylation RNA metabolic process primary metabolic process amino acid metabolic process translation gene expression tRNA aminoacylation for protein translation macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process nucleobase-containing compound metabolic process biosynthetic process metabolic process cellular process macromolecule metabolic process protein metabolic process leucyl-tRNA aminoacylation	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR023356	Leucyl-tRNA synthetase, domain 3	Domain
A	IPR025709	Leucyl-tRNA synthetase, editing domain	Domain
A	IPR001412	Aminoacyl-tRNA synthetase, class I, conserved site	Conserved Site
A	IPR015413	Methionyl/Leucyl tRNA synthetase	Domain
A	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily
A	IPR002300	Aminoacyl-tRNA synthetase, class Ia	Domain
A	IPR009008	Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain	Homologous Superfamily
A	IPR009080	Aminoacyl-tRNA synthetase, class Ia, anticodon-binding	Homologous Superfamily
A	IPR013155	Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding	Domain
A	IPR002302	Leucine-tRNA ligase	Family

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.