1CMK

CRYSTAL STRUCTURES OF THE MYRISTYLATED CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE REVEAL OPEN AND CLOSED CONFORMATIONS

Summary for 1CMK

DescriptorcAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT, cAMP-dependent protein kinase inhibitor, alpha form, MYRISTIC ACID, ... (4 entities in total)
Functional Keywordsphosphotransferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological sourceSus scrofa (pig)
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Cellular locationCytoplasm P00517
Total number of polymer chains2
Total molecular weight43640.29
Authors
Zheng, J.,Knighton, D.R.,Xuong, N.-H.,Taylor, S.S.,Sowadski, J.M.,Ten Eyck, L.F. (deposition date: 1993-11-18, release date: 1994-05-31, Last modification date: 2012-07-18)
Primary citation
Zheng, J.,Knighton, D.R.,Xuong, N.H.,Taylor, S.S.,Sowadski, J.M.,Ten Eyck, L.F.
Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations.
Protein Sci., 2:1559-1573, 1993
PubMed: 8251932 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.9 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers263.3%15.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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