› 3tm1

X-ray diffraction
1.8Å resolution

Crystal structure of mature ThnT, a pantetheine hydrolase

Released:
DOI: 10.2210/pdb3tm1/pdb
PDB entry 3tm1 coloured by chain, front view.
PDB entry 3tm1 coloured by chain, side view.
PDB entry 3tm1 coloured by chain, top view.
Source organism: Streptomyces cattleya
Primary publication:
Autoproteolytic activation of ThnT results in structural reorganization necessary for substrate binding and catalysis.
Buller AR, Labonte JW, Freeman MF, Wright NT, Schildbach JF, Townsend CA
OpenAccess logo J Mol Biol 422 508-18 (2012)
PMID: 22706025

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-182979 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 419 amino acids
Theoretical weight: 41.37 KDa
Source organism: Streptomyces cattleya
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83XN4 (Residues: 1-399; Coverage: 100%)
Sequence domains: Peptidase family S58
Structure domains: L-amino peptidase D-ALA esterase/amidase

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P21212
Unit cell:
a: 141.648Å b: 67.765Å c: 73.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.197
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Bacterial β-aminopeptidases: structural insights and applications for biocatalysis.
Heck et al. (2012)
6 other articles

3 mentions without citation

Direct association of ligand-binding and pore domains in homo- and heterotetrameric inositol 1,4,5-trisphosphate receptors.
Boehning et al. (2000)
2 more