1h4q Summary



The structure was published by Yaremchuk, A., Tukalo, M., Grotli, M., and Cusack, S., in 2001 in a paper entitled "A Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2001.

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

This PDB entry contains a complex of 2 biomacromolecules, namely PROLYL-TRNA SYNTHETASE and TRNAPRO(CGG).

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 heterotrimers.

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 PROLYL-TRNA SYNTHETASE Q5SM28 (1-477) (SYP_THET8)search Thermus thermophilus HB8search 100% 477 97%
B PROLYL-TRNA SYNTHETASE Q5SM28 (1-477) (SYP_THET8)search Thermus thermophilus HB8search 100% 477 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q5SM28 (1 - 477) PROLYL-TRNA SYNTHETASE Thermus thermophilus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q5SM28) Anticodon-binding domain of Class II aaRSsearch, Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domainsearch, C-terminal domain of ProRSsearch Bira Bifunctional Protein; Domain 2search, Rossmann foldsearch, Translation Initiation Factor IF3search PF00587: tRNA synthetase class II core domain (G, H, P, S and T)search, PF03129: Anticodon binding domainsearch, PF09180: Prolyl-tRNA synthetase, C-terminalsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (Q5SM28) tRNA aminoacylation for protein translationsearch prolyl-tRNA aminoacylationsearch translationsearch proline-tRNA ligase activitysearch aminoacyl-tRNA ligase activitysearch ATP bindingsearch nucleotide bindingsearch metal ion bindingsearch ligase activitysearch cytoplasmsearch

Chain InterPro annotation
A, B Aminoacyl-tRNA synthetase, class II (G/ H/ P/ S), conserved domainsearch Proline-tRNA ligase, class IIasearch Anticodon-bindingsearch Proline-tRNA ligase, class IIa, archaeal-typesearch Aminoacyl-tRNA synthetase, class IIsearch Proline-tRNA ligase, class II, C-terminalsearch Prolyl-tRNA synthetase, class IIsearch