5eri

X-ray diffraction
2.3Å resolution

MarR Protein from Peptoclostridium difficile DA00132

Released:
Source organism: Clostridioides difficile
Primary publication:
Crystal structure of the multiple antibiotic resistance regulator MarR from Clostridium difficile.
Acta Crystallogr F Struct Biol Commun 73 363-368 (2017)
PMID: 28580925

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HTH marR-type domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 19.55 KDa
Source organism: Clostridioides difficile
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A0A031WDA8 (Residues: 2-149; Coverage: 99%)
Gene names: BN1095_480068, BN1096_310072, BN1097_320071, E5F32_12595, E5F39_02580, IB136_2087, SAMEA3374989_02045, SAMEA3375037_02055, SAMEA3375041_01740, yybA
Sequence domains: MarR family
Structure domains: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P43212
Unit cell:
a: 66.569Å b: 66.569Å c: 83.654Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.212 0.25
Expression system: Escherichia coli BL21