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5IAJ

Caspase 3 V266L

Summary for 5IAJ
Entry DOI10.2210/pdb5iaj/pdb
Related PRD IDPRD_000238
DescriptorCaspase-3, ACE-ASP-GLU-VAL-ASK, SODIUM ION, ... (4 entities in total)
Functional Keywordsallostery, saturation mutagenesis, conformational selection, native ensemble, protein solvation, protein structure, protein dynamics, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm: P42574
Total number of polymer chains2
Total formula weight32337.06
Authors
Maciag, J.J.,Mackenzie, S.H.,Tucker, M.B.,Schipper, J.L.,Swartz, P.D.,Clark, A.C. (deposition date: 2016-02-21, release date: 2016-10-26)
Primary citationMaciag, J.J.,Mackenzie, S.H.,Tucker, M.B.,Schipper, J.L.,Swartz, P.,Clark, A.C.
Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection.
Proc.Natl.Acad.Sci.USA, 113:E6080-E6088, 2016
Cited by
PubMed: 27681633
DOI: 10.1073/pnas.1603549113
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.58 Å)
Structure validation

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