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X-ray diffraction
2Å resolution

Crystal Structure of Polyamine Aminopropyltransfease from Thermus thermophilus

Released:

Function and Biology Details

Reactions catalysed:
S-adenosylmethioninamine + agmatine = S-methyl-5'-thioadenosine + N(1)-(3-aminopropyl)agmatine
S-adenosyl 3-(methylthio)propylamine + norspermidine = S-methyl-5'-thioadenosine + norspermine
S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + spermine
S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + thermospermine + H(+)
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-178059 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyamine aminopropyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 36.09 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SK28 (Residues: 1-314; Coverage: 100%)
Gene names: TTHA0824, speE
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P43212
Unit cell:
a: 87.775Å b: 87.775Å c: 190.825Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.239
Expression system: Escherichia coli