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PDBsum entry 1tyc

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protein links
Aminoacyl-tRNA synthase PDB id
1tyc
Jmol
Contents
Protein chain
317 a.a. *
Waters ×171
* Residue conservation analysis
PDB id:
1tyc
Name: Aminoacyl-tRNA synthase
Title: Structural analysis of a series of mutants of tyrosyl-tRNA s enhancement of catalysis by hydrophobic interactions
Structure: Tyrosyl-tRNA synthetase. Chain: a. Engineered: yes
Source: Geobacillus stearothermophilus. Organism_taxid: 1422
Biol. unit: Dimer (from PQS)
Resolution:
2.50Å     R-factor:   0.219    
Authors: K.A.Brown,P.Brick,P.De Meester,D.M.Blow
Key ref: K.A.Brown et al. Structural analysis of a series of mutants of tyrosyl-Trna synthetase: enhancement of catalysis by hydrophobic interactions. To be published, .
Date:
06-Jul-92     Release date:   31-Jan-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00952  (SYY_GEOSE) -  Tyrosine--tRNA ligase
Seq:
Struc:
419 a.a.
317 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.6.1.1.1  - Tyrosine--tRNA ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
ATP
+ L-tyrosine
+ tRNA(Tyr)
= AMP
+ diphosphate
+ L-tyrosyl-tRNA(Tyr)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     tRNA aminoacylation for protein translation   2 terms 
  Biochemical function     nucleotide binding     4 terms