1tde Summary

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CRYSTAL STRUCTURE OF ESCHERICHIA COLI THIOREDOXIN REDUCTASE REFINED AT 2 ANGSTROM RESOLUTION: IMPLICATIONS FOR A LARGE CONFORMATIONAL CHANGE DURING CATALYSIS

The structure was published by Waksman, G., Krishna, T.S., Williams Jr., C.H., and Kuriyan, J., in 1994 in a paper entitled "Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1994.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of THIOREDOXIN REDUCTASE. This molecule has the UniProt identifier P0A9P4 (TRXB_ECOLI)search. The sample contained 316 residues which is 98% of the natural sequence. Out of 316 residues 315 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homodimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A THIOREDOXIN REDUCTASE P0A9P4 (2-317) (TRXB_ECOLI)search Escherichia coli K-12search 98% 316 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P0A9P4 (2 - 317) THIOREDOXIN REDUCTASE Escherichia coli

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P0A9P4) FAD/NAD-linked reductases, N-terminal and central domainssearch FAD/NAD(P)-binding domainsearch PF07992: Pyridine nucleotide-disulphide oxidoreductasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P0A9P4) oxidation-reduction processsearch removal of superoxide radicalssearch oxidoreductase activitysearch flavin adenine dinucleotide bindingsearch protein bindingsearch thioredoxin-disulfide reductase activitysearch cytoplasmsearch

Chain InterPro annotation
A Pyridine nucleotide-disulphide oxidoreductase, class-IIsearch Pyridine nucleotide-disulphide oxidoreductase, NAD-binding domainsearch Thioredoxin reductasesearch Pyridine nucleotide-disulphide oxidoreductase, class-II, active sitesearch FAD-dependent pyridine nucleotide-disulphide oxidoreductasesearch Pyridine nucleotide-disulphide oxidoreductase, FAD/NAD(P)-binding domainsearch