Structure analysis

The Crystal Structure of the N-terminal domain of a RpiR Transcriptional Regulator from Staphylococcus epidermidis to 1.4A

X-ray diffraction
1.4Å resolution
Assemblies composition:
homo dimer (preferred)
monomeric
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: homo dimer
Accessible surface area: 10300 Å2
Buried surface area: 2900 Å2
Dissociation area: 700 Å2
Dissociation energy (ΔGdiss): 1 kcal/mol
Dissociation entropy (TΔSdiss): 11 kcal/mol
Interface energy (ΔGint): -43 kcal/mol
Symmetry number: 1
Assembly 2
Download    3D Visualisation
Multimeric state: monomeric

Binding statistics and energies are not available for this assembly
Assembly 3
Download    3D Visualisation
Multimeric state: monomeric

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B
Length: 107 amino acids
Theoretical weight: 12.43 KDa
Source organism: Staphylococcus epidermidis ATCC 12228
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2VHQ2 (Residues: 1-107; Coverage: 37%)
Gene name: SE_1891
Pfam: Helix-turn-helix domain, rpiR family
InterPro:
CATH: Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain

Search similar proteins