PDBe 1jen

X-ray diffraction
2.25Å resolution

HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO(2). 
Biological process:
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 Chains: B, D
Molecule details ›
Chains: B, D
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 Chains: A, C
Molecule details ›
Chains: A, C
Length: 267 amino acids
Theoretical weight: 30.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17707 (Residues: 69-334; Coverage: 80%)
Gene names: AMD, AMD1
Structure domains: S-adenosylmethionine decarboxylase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21
Unit cell:
a: 74.6Å b: 55.8Å c: 90.1Å
α: 90° β: 109.6° γ: 90°
R-values:
R R work R free
0.177 0.177 0.229
Expression system: Escherichia coli