2CXI

Crystal Structure Of An N-terminal Fragment Of The Phenylalanyl-tRNA Synthetase Beta-Subunit From Pyrococcus Horikoshii

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF03483	e2cxiA2	A: beta complex topology	X: PheT/TilS domain (From Topology)	H: PheT/TilS domain (From Topology)	T: PheT/TilS domain	F: PF03483	ECOD (1.6)
A	PF03484	e2cxiA4	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF03484	ECOD (1.6)
A	PF18262	e2cxiA5	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF18262	ECOD (1.6)
B	PF03483	e2cxiB3	A: beta complex topology	X: PheT/TilS domain (From Topology)	H: PheT/TilS domain (From Topology)	T: PheT/TilS domain	F: PF03483	ECOD (1.6)
B	PF03484	e2cxiB4	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF03484	ECOD (1.6)
B	PF18262	e2cxiB5	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF18262	ECOD (1.6)
C	PF03483	e2cxiC3	A: beta complex topology	X: PheT/TilS domain (From Topology)	H: PheT/TilS domain (From Topology)	T: PheT/TilS domain	F: PF03483	ECOD (1.6)
C	PF03484	e2cxiC4	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF03484	ECOD (1.6)
C	PF18262	e2cxiC5	A: alpha arrays	X: HTH	H: HTH	T: Putative DNA-binding domain	F: PF18262	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.56.10	Alpha Beta	2-Layer Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 1	CATH (4.3.0)
A	3.50.40.10	Alpha Beta	3-Layer(bba) Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 3	CATH (4.3.0)
B	3.30.56.10	Alpha Beta	2-Layer Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 1	CATH (4.3.0)
B	3.50.40.10	Alpha Beta	3-Layer(bba) Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 3	CATH (4.3.0)
C	3.30.56.10	Alpha Beta	2-Layer Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 1	CATH (4.3.0)
C	3.50.40.10	Alpha Beta	3-Layer(bba) Sandwich	Phenylalanyl-tRNA Synthetase	Chain B, domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF03483	B3/4 domain (B3_4)	B3/4 domain	This domain is found in tRNA synthetase beta subunits as well as in some non tRNA synthetase proteins.	Domain
A, B, C	PF03484	tRNA synthetase B5 domain (B5)	tRNA synthetase B5 domain	This domain is found in phenylalanine-tRNA synthetase beta subunits.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Phenylalanyl-tRNA synthetase beta chain	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding ligase activity, forming carbon-oxygen bonds aminoacyl-tRNA ligase activity catalytic activity, acting on RNA catalytic activity, acting on a nucleic acid phenylalanine-tRNA ligase activity catalytic activity, acting on a tRNA catalytic activity ligase activity RNA binding nucleic acid binding	amino acid activation tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process RNA metabolic process amino acid metabolic process nucleobase-containing compound metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process translation amino acid activation tRNA aminoacylation cellular biosynthetic process organonitrogen compound biosynthetic process RNA metabolic process amino acid metabolic process nucleobase-containing compound metabolic process organic substance metabolic process organic substance biosynthetic process protein metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process translation gene expression tRNA aminoacylation for protein translation macromolecule biosynthetic process nucleic acid metabolic process tRNA metabolic process organic cyclic compound metabolic process biosynthetic process ncRNA metabolic process metabolic process cellular process macromolecule metabolic process phenylalanyl-tRNA aminoacylation	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR009061	Putative DNA-binding domain superfamily	Homologous Superfamily
A, B, C	IPR045060	Phenylalanine-tRNA ligase, class IIc, beta subunit	Family
A, B, C	IPR020825	Phenylalanyl-tRNA synthetase-like, B3/B4	Homologous Superfamily
A, B, C	IPR045864	Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)	Homologous Superfamily
A, B, C	IPR004531	Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archaeal/eukaryotic type	Family
A, B, C	IPR005147	tRNA synthetase, B5-domain	Domain
A, B, C	IPR005146	B3/B4 tRNA-binding domain	Domain
A, B, C	IPR022918	Phenylalanine-tRNA ligase beta chain 2, archaeal type	Family
A, B, C	IPR041616	Phenylalanyl tRNA synthetase beta chain, core domain	Domain

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.