Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation

2-O-octyl-beta-D-glucose; 2-O-octyl-D-glucose; 2-O-octyl-glucose

Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation.

Two non-proline cis peptide bonds may be important for factor XIII function

Three-dimensional structure of a transglutaminase: human blood coagulation factor XII

Protein-glutamine glutamyltransferase E3

pET 11a vector(Novagen) PVL1392 (Invitrogen)

4-12% (w/v) Peg 6K, 100 mM Bicine (pH 9) and 1% dioxane, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K

This is the activated form bound to three calcium ions while 1L9M is the zymogen form.

The following residues are noted as conflicts in the Swiss-Prot database: T13K, K562R, G654R. According to the author, residue 250 is Asp and does not represent a mutation but a mistake in the Swiss-Prot database.

This sequence occurs naturally in humans

NCS two fold averaging was employed during refinement but at the later stage the NCS was released

Activation, Calcium binding, transglutaminase, Transferase