4HN2

Crystal structure of the catalytic domain of human diphosphoinositol pentakisphosphate kinase 2 (PPIP5K2) in complex with AMPPNP and a substrate analog 5PA-IP5

Replaces:  4GB4

Summary for 4HN2

• Entry DOI: 10.2210/pdb4hn2/pdb
• Related: 3T9B 3T9D
• Descriptor: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, (2-oxo-2-{[(1s,2R,3S,4s,5R,6S)-2,3,4,5,6-pentakis(phosphonooxy)cyclohexyl]oxy}ethyl)phosphonic acid, ... (5 entities in total)
• Functional Keywords: atp-grasp fold, inositol pyrophosphate kinase, phosphoryl transferase, pyrophosphate analog, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol: O43314
• Total number of polymer chains: 1
• Total formula weight: 38874.38

Authors

Wang, H. (deposition date: 2012-10-18, release date: 2012-10-31, Last modification date: 2023-09-20)

Primary citation

Riley, A.M.,Wang, H.,Weaver, J.D.,Shears, S.B.,Potter, B.V.
First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP(5) kinase.
Chem.Commun.(Camb.), 48:11292-11294, 2012

PubMed Abstract: We synthesised analogues of diphosphoinositol polyphosphates (PP-InsPs) in which the diphosphate is replaced by an α-phosphonoacetic acid (PA) ester. Structural analysis revealed that 5-PA-InsP(5) mimics 5-PP-InsP(5) binding to the kinase domain of PPIP5K2; both molecules were phosphorylated by the enzyme. PA-InsPs are promising candidates for further studies into the biology of PP-InsPs.

PubMed: 23032903
DOI: 10.1039/c2cc36044f

Experimental method

X-RAY DIFFRACTION (1.9 Å)