2hcj

X-ray diffraction
2.12Å resolution

Trypsin-modified Elongation Factor Tu in complex with tetracycline

Released:
Source organism: Escherichia coli
Primary publication:
Molecular complementarity between tetracycline and the GTPase active site of elongation factor Tu.
Acta Crystallogr D Biol Crystallogr 62 1392-400 (2006)
PMID: 17057344

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143209 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Elongation factor Tu 1 Chain: A
Molecule details ›
Chain: A
Length: 37 amino acids
Theoretical weight: 3.77 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0CE47 (Residues: 9-45; Coverage: 9%)
Gene names: JW3301, b3339, tufA
Elongation factor Tu 1 Chain: B
Molecule details ›
Chain: B
Length: 335 amino acids
Theoretical weight: 36.98 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0CE47 (Residues: 60-394; Coverage: 85%)
Gene names: JW3301, b3339, tufA
Sequence domains:
Structure domains:

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43212
Unit cell:
a: 69.11Å b: 69.11Å c: 157.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.234