1LR4
Room Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays
Replaces: 1A6OSummary for 1LR4
Entry DOI | 10.2210/pdb1lr4/pdb |
Related | 1DAW 1DAY 1JWH 1LP4 1LPU 1QF8 |
Descriptor | Protein kinase CK2, BENZAMIDINE (3 entities in total) |
Functional Keywords | protein kinase, ck2, casein kinase 2, dual-cosubstrate specificity, transferase |
Biological source | Zea mays |
Total number of polymer chains | 1 |
Total formula weight | 39411.32 |
Authors | Niefind, K.,Puetter, M.,Guerra, B.,Issinger, O.-G.,Schomburg, D. (deposition date: 2002-05-14, release date: 2002-05-29, Last modification date: 2023-10-25) |
Primary citation | Yde, C.W.,Ermakova, I.,Issinger, O.G.,Niefind, K. Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate. J.Mol.Biol., 347:399-414, 2005 Cited by PubMed: 15740749DOI: 10.1016/j.jmb.2005.01.003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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