› 1msv

X-ray diffraction
1.75Å resolution

The S68A S-adenosylmethionine decarboxylase proenzyme processing mutant.

Released:
DOI: 10.2210/pdb1msv/pdb
PDB entry 1msv coloured by chain, front view.
PDB entry 1msv coloured by chain, side view.
PDB entry 1msv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanism of human S-adenosylmethionine decarboxylase proenzyme processing as revealed by the structure of the S68A mutant.
Tolbert WD, Zhang Y, Cottet SE, Bennett EM, Ekstrom JL, Pegg AE, Ealick SE
Biochemistry 42 2386-95 (2003)
PMID: 12600205

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148141 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
S-adenosylmethionine decarboxylase proenzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 354 amino acids
Theoretical weight: 40.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17707 (Residues: 1-334; Coverage: 100%)
Gene names: AMD, AMD1
Sequence domains: Adenosylmethionine decarboxylase
Structure domains: S-adenosylmethionine decarboxylase

Ligands and Environments

2 bound ligands:
Ligand PUT 2 x PUT
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21
Unit cell:
a: 73.936Å b: 56.382Å c: 99.19Å
α: 90° β: 110.97° γ: 90°
R-values:
R R work R free
0.22 0.21 0.238
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Functions of Polyamines in Mammals.
Pegg AE. (2016)
8 more

6 mentions without citation

Structural biology of S-adenosylmethionine decarboxylase.
Bale et al. (2010)
5 more