X-ray diffraction
1.55Å resolution

Crystal Structure of Thermotoga maritima S-adenosylmethionine decarboxylase


Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO(2)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
S-adenosylmethionine decarboxylase proenzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.81 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
  • Canonical: Q9WZC3 (Residues: 1-130; Coverage: 100%)
Gene names: TM_0655, speH
Sequence domains: S-adenosylmethionine decarboxylase
Structure domains: S-adenosylmethionine decarboxylase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 8-BM
Spacegroup: R3
Unit cell:
a: 104.994Å b: 104.994Å c: 69.695Å
α: 90° β: 90° γ: 120°
R R work R free
0.155 0.152 0.187
Expression system: Escherichia coli