1LR4

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

Replaces:  1A6O

Summary for 1LR4

Related1LPU 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: 2002-05-14, release date: 2002-05-29, Last modification date: 2017-10-11)
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 (2 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.2421403.0%5.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 1lr4
no rotation
Molmil generated image of 1lr4
rotated about x axis by 90°
Molmil generated image of 1lr4
rotated about y axis by 90°