PDBe 3ep8

X-ray diffraction
1.97Å resolution

Human AdoMetDC E178Q mutant complexed with S-Adenosylmethionine methyl ester and no putrescine bound

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
S-adenosylmethionine decarboxylase beta chain Chain: B
Molecule details ›
Chain: B
Length: 67 amino acids
Theoretical weight: 7.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17707 (Residues: 1-67; Coverage: 20%)
Gene names: AMD, AMD1
Structure domains: S-adenosylmethionine decarboxylase
S-adenosylmethionine decarboxylase alpha chain Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 29.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17707 (Residues: 69-328; Coverage: 78%)
Gene names: AMD, AMD1
Structure domains: S-adenosylmethionine decarboxylase

Ligands and Environments


Cofactor: Ligand SMM 1 x SMM
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 100.146Å b: 51.073Å c: 68.947Å
α: 90° β: 105.39° γ: 90°
R-values:
R R work R free
0.209 0.209 0.237
Expression system: Escherichia coli