1LPU

Low Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays

Summary for 1LPU

Related1LR4 1LP4 1DAW 1DAY 1JWH 1QF8
DescriptorProtein kinase CK2, BENZAMIDINE (3 entities in total)
Functional Keywordsprotein kinase, ck2, casein kinase 2, dual-cosubstrate specificity, transferase
Biological sourceZea mays
Total number of polymer chains1
Total molecular weight39411.32
Authors
Niefind, K.,Puetter, M.,Guerra, B.,Issinger, O.-G.,Schomburg, D. (deposition date: 2002-05-08, release date: 2002-05-29, Last modification date: 2011-07-13)
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
PubMed: 15740749 (PDB entries with the same primary citation)
DOI: 10.1016/j.jmb.2005.01.003
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.86 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.2581403.0%4.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 1lpu
no rotation
Molmil generated image of 1lpu
rotated about x axis by 90°
Molmil generated image of 1lpu
rotated about y axis by 90°