1euy Summary

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GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN ACTIVE SITE INHIBITOR

The structure was published by Sherlin, L.D., Bullock, T.L., Newberry, K.J., et al., Beijer, B., Sproat, B.S., and Perona, J.J., in 2000 in a paper entitled "Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2000.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely GLUTAMINYL TRNA and GLUTAMINYL-TRNA SYNTHETASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms heterodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A GLUTAMINYL-TRNA SYNTHETASE P00962 (1-548) (SYQ_ECOLI)search Escherichia coli K-12search 97% 548 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00962 (1 - 548) GLUTAMINYL-TRNA SYNTHETASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00962) Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domainsearch, Class I aminoacyl-tRNA synthetases (RS), catalytic domainsearch Ribosomal Protein L25; Chain Psearch, Glutamyl-trna Synthetase; Domain 2search, Glutamyl-tRNA Synthetase; Domain 3search, HUPssearch PF00749: tRNA synthetases class I (E and Q), catalytic domainsearch, PF03950: tRNA synthetases class I (E and Q), anti-codon binding domainsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P00962) ATP bindingsearch ligase activity, forming aminoacyl-tRNA and related compoundssearch nucleotide bindingsearch aminoacyl-tRNA ligase activitysearch glutamine-tRNA ligase activitysearch ligase activitysearch cytoplasmsearch tRNA aminoacylationsearch tRNA aminoacylation for protein translationsearch glutaminyl-tRNA aminoacylationsearch translationsearch glutamyl-tRNA aminoacylationsearch

Chain InterPro annotation
A Glutamyl/glutaminyl-tRNA synthetasesearch Aminoacyl-tRNA synthetase, class I, conserved sitesearch Glutamine-tRNA synthetasesearch Ribosomal protein L25/Gln-tRNA synthetase, anti-codon-binding domainsearch Rossmann-like alpha/beta/alpha sandwich foldsearch Ribosomal protein L25/Gln-tRNA synthetase, beta-barrel domainsearch Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domainsearch Glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domainsearch Glutamyl/glutaminyl-tRNA synthetase, class Ib, alpha-bundle domainsearch Glutamine-tRNA ligase, bacterialsearch