X-ray diffraction
2.7Å resolution

Crystal structure of the N-terminal domain of TagH from Bacillus subtilis


Function and Biology Details

Reaction catalysed:
ATP + H(2)O + teichoic acid(Side 1) = ADP + phosphate + teichoic acid(Side 2)
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
Teichoic acids export ATP-binding protein TagH Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 280 amino acids
Theoretical weight: 32.18 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
  • Canonical: P42954 (Residues: 1-280; Coverage: 53%)
Gene names: BSU35700, tagH
Sequence domains: ABC transporter

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL15A1
Spacegroup: P21
Unit cell:
a: 73.735Å b: 90.667Å c: 91.213Å
α: 90° β: 91.766° γ: 90°
R R work R free
0.189 0.186 0.235
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'