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6BDV

Crystal structure of Caspase 3 S150A

Summary for 6BDV
Entry DOI10.2210/pdb6bdv/pdb
Related PRD IDPRD_000238
DescriptorCaspase-3 subunit p17, Caspase-3 subunit p12, Acetyl-Asp-Glu-Val-Asp-CMK, ... (6 entities in total)
Functional Keywordsallosteric regulation, biophysics, caspase, computational biology, fluorescence, molecular dynamics, protein evolution, apoptosis
Biological sourceHomo sapiens (Human)
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Cellular locationCytoplasm: P42574 P42574
Total number of polymer chains3
Total formula weight32308.39
Authors
Thomas, M.E.,Grinshpon, R.,Swartz, P.D.,Clark, A.C. (deposition date: 2017-10-24, release date: 2018-02-14, Last modification date: 2018-04-25)
Primary citationThomas, M.E.,Grinshpon, R.,Swartz, P.,Clark, A.C.
Modifications to a common phosphorylation network provide individualized control in caspases.
J. Biol. Chem., 293:5447-5461, 2018
Cited by
PubMed: 29414778
DOI: 10.1074/jbc.RA117.000728
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.938 Å)
Structure validation

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