3c6k

X-ray diffraction
1.95Å resolution

Crystal structure of human spermine synthase in complex with spermidine and 5-methylthioadenosine

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + spermine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spermine synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 381 amino acids
Theoretical weight: 43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P52788 (Residues: 5-366; Coverage: 99%)
Gene name: SMS
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P1
Unit cell:
a: 43.385Å b: 74.032Å c: 143.226Å
α: 94.23° β: 92.88° γ: 107.07°
R-values:
R R work R free
0.201 0.198 0.257
Expression system: Escherichia coli