› 1ub9

X-ray diffraction
2.05Å resolution

Structure of the transcriptional regulator homologue protein from Pyrococcus horikoshii OT3

Released:
DOI: 10.2210/pdb1ub9/pdb
PDB entry 1ub9 coloured by chain, front view.
PDB entry 1ub9 coloured by chain, side view.
PDB entry 1ub9 coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Structural analysis of the transcriptional regulator homolog protein from Pyrococcus horikoshii OT3.
Okada U, Sakai N, Yao M, Watanabe N, Tanaka I
Proteins 63 1084-6 (2006)
PMID: 16506234

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129768 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HTH arsR-type domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 11.4 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58788 (Residues: 1-100; Coverage: 100%)
Gene name: PH1061
Sequence domains: Winged helix DNA-binding domain
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: SPRING-8 BEAMLINE BL41XU
Spacegroup: P43212
Unit cell:
a: 45.159Å b: 45.159Å c: 96.175Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.242
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Metal homeostasis in bacteria: the role of ArsR-SmtB family of transcriptional repressors in combating varying metal concentrations in the environment.
Saha et al. (2017)
3 other articles

1 mention without citation

Intrinsically disordered regions may lower the hydration free energy in proteins: a case study of nudix hydrolase in the bacterium Deinococcus radiodurans.
Awile et al. (2010)