› 3a8t

X-ray diffraction
2.37Å resolution

Plant adenylate isopentenyltransferase in complex with ATP

Released:
DOI: 10.2210/pdb3a8t/pdb
PDB entry 3a8t coloured by chain, front view.
PDB entry 3a8t coloured by chain, side view.
PDB entry 3a8t coloured by chain, top view.
Source organism: Humulus lupulus
Primary publication:
Crystal structure and substrate specificity of plant adenylate isopentenyltransferase from Humulus lupulus: distinctive binding affinity for purine and pyrimidine nucleotides.
Chu HM, Ko TP, Wang AH
Nucleic Acids Res 38 1738-48 (2010)
PMID: 20007608

Function and Biology Details

Reactions catalysed: 
Prenyl diphosphate + ADP = diphosphate + N6-prenyladenosine diphosphate
Prenyl diphosphate + AMP = diphosphate + N(6)-prenyladenosine 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177147 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenylate isopentenyltransferase Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 37.92 KDa
Source organism: Humulus lupulus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5GHF7 (Residues: 1-329; Coverage: 100%)
Gene name: AIPT
Sequence domains: IPP transferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ATP 1 x ATP
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 45.422Å b: 75.887Å c: 81.128Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.235
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Evolution of cytokinin biosynthesis and degradation.
Frébort et al. (2011)
4 more

1 mention without citation

Distinct Conformation of ATP Molecule in Solution and on Protein.
Kobayashi et al. (2013)