X-ray diffraction
2.1Å resolution

Crystal Structure of adenosine phosphate-isopentenyltransferase complexed with substrate analog, DMASPP

Source organism: Agrobacterium tumefaciens
Primary publication:
Structural insight into the reaction mechanism and evolution of cytokinin biosynthesis.
Proc. Natl. Acad. Sci. U.S.A. 105 2734-9 (2008)
PMID: 18258747

Function and Biology Details

Reaction catalysed:
Dimethylallyl diphosphate + AMP = diphosphate + N(6)-(dimethylallyl)adenosine 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Adenylate dimethylallyltransferase Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 28.84 KDa
Source organism: Agrobacterium tumefaciens
Expression system: Escherichia coli
  • Canonical: P58758 (Residues: 1-243; Coverage: 100%)
Gene names: AGR_pTi_290, Atu6164, tzs
Sequence domains: Isopentenyl transferase
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45PX
Spacegroup: P42212
Unit cell:
a: 96.417Å b: 96.417Å c: 65.068Å
α: 90° β: 90° γ: 90°
R R work R free
0.2 0.196 0.264
Expression system: Escherichia coli