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. 2008 Jun 6;379(3-2):520–534. doi: 10.1016/j.jmb.2008.03.077

Table 2.

Thioredoxin complex structures used in this study

PDB code Thioredoxin (mutation) Trx catalytic residue: substrate target residue Other proteins in complex (mutation) Method Resolution (Å) Reference
Thioredoxin–substrate complexes
1MDJ Human Trx (C35A, C65A, C69A, C73A) C32 : C62 Peptide consisting of residues 56–68 from the human substrate NF-κB NMR N/A 14
1CQG Human Trx C32 : C65 Peptide consisting of residues 59–71 from the human substrate Ref-1 NMR N/A 15
1CQH (C35A, C65A, C69A, C73A)
2IWT Barley HvTrxh2 (C49S) C46 : C148 α-Amylase serine proteinase inhibitor (BASI) (C144S) X-ray 2.3 16
2IPA BsTrxA (C32S) C29 : C89 ArsC (C10S, C15A, C82S) NMR N/A 12
2VOC BsTrxA (C32S) C29 : C29 BsTrxA (C32S) homodimer X-ray 1.5 This study



Thioredoxin–thioredoxin reductase complexes
2PU9 Spinach chloroplast (Trx-f) (C49S) C46 : C57 Synechocystis ferrodoxin–thioredoxin reductase X-ray 1.65 20
2PUK Spinach chloroplast (Trx-m) (C40S) C37 : C57 Synechocystis ferrodoxin–thioredoxin reductase X-ray 3.0 20
1F6M E. coli TrxA (C35S) C32 : C138 E. coli thioredoxin reductase (C135S) X-ray 3.0 19



Other thioredoxin complexes
1T7P E. coli TrxA N/A Bacteriophage T7 DNA polymerase and an DNA strand X-ray 2.2 21

N/A, not available.

Structural data were retrieved from the PDB. The accession codes, relevant mutations, catalytic residues, interacting proteins, and structure analysis details are summarized.