› 2o05

X-ray diffraction
2Å resolution

Human spermidine synthase

Released:
DOI: 10.2210/pdb2o05/pdb
PDB entry 2o05 coloured by chain, front view.
PDB entry 2o05 coloured by chain, side view.
PDB entry 2o05 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and mechanism of spermidine synthases.
Wu H, Min J, Ikeguchi Y, Zeng H, Dong A, Loppnau P, Pegg AE, Plotnikov AN
Biochemistry 46 8331-9 (2007)
PMID: 17585781

Function and Biology Details

Reaction catalysed: 
S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl-5'-thioadenosine + spermidine
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-148670 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spermidine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19623 (Residues: 1-302; Coverage: 100%)
Gene names: SPS1, SRM, SRML1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MTA 2 x MTA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 57.931Å b: 60.529Å c: 86.641Å
α: 90° β: 108.42° γ: 90°
R-values:
R R work R free
0.194 0.191 0.249
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Mammalian polyamine metabolism and function.
Pegg AE. (2009)
17 more

2 mentions without citation

Crystal structure of thermospermine synthase from Medicago truncatula and substrate discriminatory features of plant aminopropyltransferases.
Sekula et al. (2018)
1 more