1vj7

X-ray diffraction
2.1Å resolution

Crystal structure of the bifunctional catalytic fragment of RelSeq, the RelA/SpoT homolog from Streptococcus equisimilis.

Released:

Function and Biology Details

Reactions catalysed:
ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate
Guanosine 3',5'-bis(diphosphate) + H(2)O = guanosine 5'-diphosphate + diphosphate
Biochemical function:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional (p)ppGpp synthase/hydrolase RelA Chains: A, B
Molecule details ›
Chains: A, B
Length: 393 amino acids
Theoretical weight: 45.61 KDa
Source organism: Streptococcus dysgalactiae subsp. equisimilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q54089 (Residues: 1-385; Coverage: 52%)
Gene names: rel, relA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: C2
Unit cell:
a: 173.49Å b: 45.45Å c: 126.47Å
α: 90° β: 109.83° γ: 90°
R-values:
R R work R free
0.238 0.236 0.272
Expression system: Escherichia coli