3H5G

Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides.

Summary for 3H5G

Entry DOI	10.2210/pdb3h5g/pdb
Related	1coi 1cos 2jgo 3H5F
Descriptor	COIL SER L16D-Pen, ZINC ION, ACETATE ION, ... (4 entities in total)
Functional Keywords	de-novo protein, parallel three-stranded coiled coil, d-penicillamine, de novo protein
Total number of polymer chains	3
Total formula weight	10578.62
Authors	Peacock, A.F.A.,Stuckey, J.A.,Pecoraro, V.L. (deposition date: 2009-04-22, release date: 2009-07-14, Last modification date: 2023-11-22)
Primary citation	Peacock, A.F.,Stuckey, J.A.,Pecoraro, V.L. Switching the Chirality of the Metal Environment Alters the Coordination Mode in Designed Peptides. Angew.Chem.Int.Ed.Engl., 48:7371-7374, 2009 Cited by PubMed Abstract: The effects of switching the chirality of a single layer of amino acids in a three stranded coiled coil has been investigated. X-ray crystallography reveals that this modification is well tolerated and does not alter the designed structure. In contrast, spectroscopic studies of cadmium binding to both the L- and D- enantiomers of the penicillamine, provide evidence that this switch dramatically alters the metal binding capability, the resulting coordination environment and the position of binding. PubMed: 19579245 DOI: 10.1002/anie.200902166 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.71 Å)

Structure validation