Navigation Tabs
Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate External Resource: Annotation Domain Annotation: SCOP2 Classification SCOP2 Database Homepage Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2 Family Class I aminoacyl-tRNA synthetases (RS) catalytic domain 8026301 4003807 SCOP2 (2022-06-29) A SCOP2 Superfamily Nucleotidylyl transferase 8038680 3001541 SCOP2 (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A F_UNCLASSIFIED e4a91A3 A: alpha bundles X: Zn-binding domain in glutaminyl-tRNA synthetase (From Topology) H: Zn-binding domain in glutaminyl-tRNA synthetase (From Topology) T: Zn-binding domain in glutaminyl-tRNA synthetase F: F_UNCLASSIFIED ECOD (1.6) A PF00749 e4a91A2 A: a/b three-layered sandwiches X: HUP domain-like H: HUP domains (From Topology) T: HUP domains F: PF00749 ECOD (1.6)
Chains Accession Name Description Comments Source PF00749 tRNA synthetases class I (E and Q), catalytic domain (tRNA-synt_1c) tRNA synthetases class I (E and Q), catalytic domain Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organisms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln). Domain
Chains Polymer Molecular Function Biological Process Cellular Component GLUTAMYL-Q TRNA(ASP) SYNTHETASE