General information
PDB ID 1GTS
Title STRUCTURAL BASIS FOR TRANSFER RNA AMINOACEYLATION BY ESCHERICHIA COLI GLUTAMINYL-TRNA SYNTHETASE
PDB header LIGASE/RNA
Date 1993-09-15
Experimental method X-RAY DIFFRACTION
Resolution (A) 2.8
Kind rna
Organism ESCHERICHIA COLI
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PDB PDBe MMDB Jena OCA
CATH PDBsum HSSP PDBePISA UniProt
ProteopediA BIPA
PRIDB
Composition of PDB entry and biounits
File: Protein chains: DNA chains: RNA chains: No. of models: Action:
PDB entry:
pdb1gts.pdb A B 0
Biounits:
1gts.pdb1.pdb A B 1
Pfam domains
Name: Type: Domain: E-value: Significance: Clan: Prot. chain: Start res.: End res.: Nuc. chains: Int. mode: Action:
tRNA-synt_1c Domain P00962_27-338 1.9e-128 1 CL0039 A 26 337 B   
tRNA-synt_1c_C Domain P00962_340-528 2.6e-59 1 No_clan A 339 527 B   
SCOP domains
Classification: Protein: Prot. chain: Start res.: End res.: Nuc. chains: Int. mode: Action:
Class: All beta proteins
  Fold: Ribosomal protein L25-like
    Superfamily: Ribosomal protein L25-like
      Family: Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain
Gln-tRNA synthetase (GlnRS), C-terminal (anticodon-binding) domain A 339 547 B -
Class: Alpha and beta proteins (a/b)
  Fold: Adenine nucleotide alpha hydrolase-like
    Superfamily: Nucleotidylyl transferase
      Family: Class I aminoacyl-tRNA synthetases (RS), catalytic domain
Glutaminyl-tRNA synthetase (GlnRS) A 8 338 B -
GO terms
Protein chains: GO type: GO description:
A=2-553 C cytoplasm
A=2-553 F glutamine-tRNA ligase activity
A=2-553 F ATP binding
A=2-553 P glutaminyl-tRNA aminoacylation
Sequences
Download file with secondary structure created by Stride  
1gts.pdb1.pdb:   [ download sequences in FASTA format ]
A (protein): 
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B (rna): 
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