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1DAY

CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-GMPPNP

Summary for 1DAY
Entry DOI10.2210/pdb1day/pdb
Related1A6O 1DAW
DescriptorPROTEIN KINASE CK2, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (4 entities in total)
Functional Keywordsprotein kinase ck2, dual-cosubstrate specificity, binary complex with mg-gmppnp, transferase
Biological sourceZea mays
Total number of polymer chains1
Total formula weight39244.20
Authors
Niefind, K.,Puetter, M.,Guerra, B.,Issinger, O.G.,Schomburg, D. (deposition date: 1999-11-01, release date: 2000-05-03, Last modification date: 2023-08-09)
Primary citationNiefind, K.,Putter, M.,Guerra, B.,Issinger, O.G.,Schomburg, D.
GTP plus water mimic ATP in the active site of protein kinase CK2.
Nat.Struct.Biol., 6:1100-1103, 1999
Cited by
PubMed Abstract: The structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP were determined to 2.2 A resolution. Unlike most other protein kinases, CK2 from various sources shows 'dual-cosubstrate specificity', that is, the ability to efficiently use either ATP or GTP as a cosubstrate. The structures of these complexes demonstrate that water molecules are critical to switch the active site of CK2 from an ATP- to a GTP-compatible state. An understanding of the structural basis of dual-cosubstrate specificity may help in the design of drugs that target CK2 or other kinases with this property.
PubMed: 10581548
DOI: 10.1038/70033
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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