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). 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):
This entry contains 1 unique UniProt protein: