2iii

X-ray diffraction
2.3Å resolution

Crystal structure of the adenosylmethionine decarboxylase (aq_254) from aquifex aeolicus vf5

Released:
Source organism: Aquifex aeolicus VF5
Entry authors: Jeyakanthan J, Kanaujia SP, Vasuki Ranjani C, Sekar K, Baba S, Ebihara A, Kuramitsu S, Shinkai A, Shiro Y, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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)
PDBe Complex ID:
PDB-CPX-130350 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine decarboxylase proenzyme Chain: A
Molecule details ›
Chain: A
Length: 135 amino acids
Theoretical weight: 15.32 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O66615 (Residues: 1-135; Coverage: 100%)
Gene names: aq_254, speH
Sequence domains: S-adenosylmethionine decarboxylase
Structure domains: S-adenosylmethionine decarboxylase

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P41212
Unit cell:
a: 41.792Å b: 41.792Å c: 134.921Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.246
Expression system: Escherichia coli