3anx

X-ray diffraction
2.5Å resolution

Crystal structure of triamine/agmatine aminopropyltransferase (SPEE) from thermus thermophilus, complexed with MTA

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

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-178060 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyamine aminopropyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 36.06 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SK28 (Residues: 1-314; Coverage: 100%)
Gene names: TTHA0824, speE
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P43212
Unit cell:
a: 88.04Å b: 88.04Å c: 191Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.18 0.263
Expression system: Escherichia coli