1ile Summary

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ISOLEUCYL-TRNA SYNTHETASE

The structure was published by Nureki, O., Vassylyev, D.G., Tateno, M., et al., Hendrickson, T.L., Schimmel, P., and Yokoyama, S., in 1998 in a paper entitled "Enzyme structure with two catalytic sites for double-sieve selection of substrate." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of ISOLEUCYL-TRNA SYNTHETASE. This molecule has the UniProt identifier P56690 (SYI_THET8)search. The sample contained 821 residues which is < 90% of the natural sequence. Out of 821 residues 821 were observed and are deposited in the PDB.

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 is most likely monomeric.

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 ISOLEUCYL-TRNA SYNTHETASE P56690 (1-821) (SYI_THET8)search Thermus thermophilus HB8search < 90% 821 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P56690 (1 - 821) ISOLEUCYL-TRNA SYNTHETASE Thermus thermophilus HB8

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetasessearch, ValRS/IleRS/LeuRS editing domainsearch, Class I aminoacyl-tRNA synthetases (RS), catalytic domainsearch HUPssearch, Isoleucyl-tRNA Synthetase; Domain 2search, Isoleucyl-tRNA Synthetase; Domain 1search tRNA synthetases class I (I, L, M and V)search, Anticodon-binding domain of tRNAsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P56690) aminoacyl-tRNA ligase activitysearch nucleotide bindingsearch ATP bindingsearch isoleucine-tRNA ligase activitysearch aminoacyl-tRNA editing activitysearch cytoplasmsearch tRNA aminoacylation for protein translationsearch isoleucyl-tRNA aminoacylationsearch

Chain InterPro annotation
A Aminoacyl-tRNA synthetase, class I, conserved sitesearch Aminoacyl-tRNA synthetase, class Iasearch Isoleucine-tRNA ligasesearch Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domainsearch Aminoacyl-tRNA synthetase, class 1a, anticodon-bindingsearch Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-bindingsearch Rossmann-like alpha/beta/alpha sandwich foldsearch