Type | Description |
---|---|
Definition | thioredoxin 1 |
Date | Results | Publications |
---|---|---|
2019-07-20 12:57:00 | Hydrophobic Residue in Escherichia coli Thioredoxin Critical for the Processivity of T7 | 30265524 |
2017-04-15 10:13:00 | By borrowing the CGPC active site of Trx-1 in combination with a T200M point mutation, we transformed DsbG into an enzyme highly reactive toward GSNO and YbiS. The pKa of the nucleophilic cysteine, as well as the redox and thermodynamic properties of the engineered DsbG are dramatically changed and become similar to those of Trx-1. | 27226614 |
2015-05-09 11:41:00 | In our model, EcTRX folding starts with structure formation in the beta-sheet, while the protein helices coalesce later. | 25463044 |
2011-03-05 11:09:00 | Data show that single amino acid mutants require higher detergent concentrations to induce secondary structure than the amount needed for wild type peptide. | 20607854 |
2010-11-06 11:00:00 | Amino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein. | 20873718 |
Type | IDs |
---|---|
Synonymous | ECK3773, dasC, fipA, tsnC |
Gene |
UniProtKB-ID:
THIO_ECOLI
UniprotKB:
P0AA25
UniParc:
UPI000003112A
EMBL:
M12779,
M26133,
M10424,
M54881,
M87049,
K02845,
U00096,
AP009048
EnsemblGenome:
BAE77517,
b3781
KO:
ecj:JW5856,
eco:b3781
|
Nucleutide sequences |
EMBL-CDS:
AAA24534.1,
AAA24694.1,
AAA24696.1,
AAC76786.2,
AAA24693.1,
AAA67582.1,
AAA24533.1,
BAE77517.1
EnsemblGenome_TRS:
AAC76786,
BAE77517
|
Protein sequencees |
EnsemblGenome_PRO:
AAC76786,
BAE77517
RefSeq:
NP_418228.2
|
Others |
UniRef100:
UniRef100_P0AA27
UniRef90:
UniRef90_P0AA27
UniRef50:
UniRef50_P0AA27
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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