Table 2.
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.