2o6c

X-ray diffraction
1.7Å resolution

Structure of selenomethionyl rTp34 from Treponema pallidum

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
34 kDa membrane antigen Chains: A, B
Molecule details ›
Chains: A, B
Length: 189 amino acids
Theoretical weight: 20.72 KDa
Source organism: Treponema pallidum
Expression system: Escherichia coli
UniProt:
  • Canonical: P19478 (Residues: 16-204; Coverage: 100%)
Gene names: TP_0971, tpd
Sequence domains: Fe2+ transport protein
Structure domains: Periplasmic metal-binding protein Tp34-type

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 34.41Å b: 66.02Å c: 150.992Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.184 0.215
Expression system: Escherichia coli