3t0y

X-ray diffraction
2.1Å resolution

Structure of the PhyR anti-anti-sigma domain bound to the anti-sigma factor, NepR

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Response regulatory domain-containing protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 142 amino acids
Theoretical weight: 15.75 KDa
Source organism: Caulobacter vibrioides
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3CBZ6 (Residues: 1-141; Coverage: 48%)
Gene names: CCNA_03591, phyR
Structure domains:
NepR domain-containing protein Chains: B, D
Molecule details ›
Chains: B, D
Length: 68 amino acids
Theoretical weight: 7.86 KDa
Source organism: Caulobacter vibrioides
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3CFC9 (Residues: 1-61; Coverage: 100%)
Gene names: CCNA_03590, nepR
Sequence domains: Anti-sigma factor NepR

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: C2221
Unit cell:
a: 75.37Å b: 105.32Å c: 97.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.2 0.251
Expression system: Escherichia coli