Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
SO4 Sulfate ion
AMO Aspartyl-adenosine-5'-monophosphate
Non-standard Residues
Code Name Show
PSU Pseudouridine-5'-monophosphate
H2U 5,6-dihydrouridine-5'-monophosphate
1MG 1n-methylguanosine-5'-monophosphate
5MC 5-methylcytidine-5'-monophosphate
5MU 5-methyluridine 5'-monophosphate
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1IL2   PDBj   RCSB PDB   PDBe
Header : LIGASE/RNA
Title : Crystal Structure of the E. coli Aspartyl-tRNA Synthetase:Yeast tRNAasp:aspartyl-Adenylate Complex
Release Data : 2001-09-28
Compound :
mol_id molecule chains
1 ASPARTYL TRANSFER RNA C,D
mol_id molecule chains
2 ASPARTYL-TRNA SYNTHETASE A,B
ec: 6.1.1.12
Source :
mol_id organism_scientific organism_common
1 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
mol_id organism_scientific expression_system
2 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
expression_system_vector_type: plasmid
expression_system_plasmid: pbr322
Authors : Moulinier, L., Eiler, S., Eriani, G., Gangloff, J., Thierry, J.C., Gabriel, K., McClain, W.H., Moras, D.
Keywords : protein-rna complex, LIGASE-RNA COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.60 Å )
Citation :

The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.

Moulinier, L.,Eiler, S.,Eriani, G.  et al.
(2001)  EMBO J.  20 : 5290 - 5301

PubMed: 11566892
DOI: 10.1093/emboj/20.18.5290

Chain : A, B
UniProt : P21889 (SYD_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L- aspartyl-tRNA(Asp) 6.1.1.12 HAMAP- Rule:MF_00044, PubMed:10918062
-