1ERW

HUMAN THIOREDOXIN DOUBLE MUTANT WITH CYS 32 REPLACED BY SER AND CYS 35 REPLACED BY SER

Summary for 1ERW

Entry DOI	10.2210/pdb1erw/pdb
Descriptor	THIOREDOXIN (2 entities in total)
Functional Keywords	dimer, oxidoreductase, thioredoxin
Biological source	Homo sapiens (human)
Cellular location	Nucleus : P10599
Total number of polymer chains	1
Total formula weight	11718.35
Authors	Weichsel, A.,Gasdaska, J.R.,Powis, G.,Montfort, W.R. (deposition date: 1996-02-07, release date: 1996-10-14, Last modification date: 2024-11-06)
Primary citation	Weichsel, A.,Gasdaska, J.R.,Powis, G.,Montfort, W.R. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure, 4:735-751, 1996 Cited by PubMed Abstract: Human thioredoxin reduces the disulfide bonds of numerous proteins in vitro, and can activate transcription factors such as NFkB in vivo. Thioredoxin can also act as a growth factor, and is overexpressed and secreted in certain tumor cells. PubMed: 8805557 DOI: 10.1016/S0969-2126(96)00079-2 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation