5mi9

X-ray diffraction
3.3Å resolution

Structure of the phosphomimetic mutant of the elongation factor EF-Tu T62E

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongation factor Tu 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 402 amino acids
Theoretical weight: 44.36 KDa
Source organism: Escherichia coli HS
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A8A5E6 (Residues: 2-394; Coverage: 100%)
Gene names: EcHS_A3535, tuf1
Sequence domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P1
Unit cell:
a: 58.12Å b: 62.1Å c: 65.47Å
α: 109.25° β: 106° γ: 88.15°
R-values:
R R work R free
0.227 0.226 0.253
Expression system: Escherichia coli BL21(DE3)