1LBK

Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme

Summary for 1LBK

Entry DOI	10.2210/pdb1lbk/pdb
Descriptor	Glutathione S-transferase class pi chimaera (CODA), 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLUTATHIONE, ... (5 entities in total)
Functional Keywords	glutathione transferase p1-1, chimaera, recombinant protein, substrate specificity, transferase
Biological source	Homo sapiens (human) More
Cellular location	Cytoplasm: P08263
Total number of polymer chains	2
Total formula weight	47578.41
Authors	Kong, G.K.W.,Micaloni, C.,Mazzetti, A.P.,Nuccetelli, M.,Antonini, G.,Stella, L.,McKinstry, W.J.,Polekhina, G.,Rossjohn, J.,Federici, G.,Ricci, G.,Parker, M.W.,Lo Bello, M. (deposition date: 2002-04-04, release date: 2002-04-17, Last modification date: 2023-08-16)
Primary citation	Micaloni, C.,Kong, G.K.W.,Mazzetti, A.P.,Nuccetelli, M.,Antonini, G.,Stella, L.,McKinstry, W.J.,Polekhina, G.,Rossjohn, J.,Federici, G.,Ricci, G.,Parker, M.W.,Lo Bello, M. Engineering a new C-terminal tail in the H-site of human glutathione transferase P1-1: structural and functional consequences. J.Mol.Biol., 325:111-122, 2003 Cited by PubMed: 12473455 DOI: 10.1016/S0022-2836(02)01178-6 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.86 Å)

Structure validation