1TRW

THE HIGH-RESOLUTION THREE-DIMENSIONAL SOLUTION STRUCTURES OF THE OXIDIZED AND REDUCED STATES OF HUMAN THIOREDOXIN

Summary for 1TRW

Entry DOI	10.2210/pdb1trw/pdb
Descriptor	THIOREDOXIN (2 entities in total)
Functional Keywords	electron transport
Biological source	Homo sapiens (human)
Cellular location	Nucleus: P10599
Total number of polymer chains	1
Total formula weight	11624.19
Authors	Clore, G.M.,Qin, J.,Gronenborn, A.M. (deposition date: 1994-05-10, release date: 1994-09-30, Last modification date: 2024-05-22)
Primary citation	Qin, J.,Clore, G.M.,Gronenborn, A.M. The high-resolution three-dimensional solution structures of the oxidized and reduced states of human thioredoxin. Structure, 2:503-522, 1994 Cited by PubMed Abstract: Thioredoxin is a ubiquitous protein and is involved in a variety of fundamental biological functions. Its active site is conserved and has two redox active cysteines in the sequence Trp-Cys-Gly-Pro-Cys. No structures of the oxidized and reduced states from the same species have been determined at high resolution under the same conditions and using the same methods. Hence, any detailed comparison of the two oxidation states has been previously precluded. PubMed: 7922028 DOI: 10.1016/S0969-2126(00)00051-4 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation