1gp1 Summary

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THE REFINED STRUCTURE OF THE SELENOENZYME GLUTATHIONE PEROXIDASE AT 0.2-NM RESOLUTION

The structure was published by Epp, O., Ladenstein, R., and Wendel, A., in 1983 in a paper entitled "The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1985.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of GLUTATHIONE PEROXIDASE.

The molecule most likely forms homotetramers.

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 GLUTATHIONE PEROXIDASE P00435 (8-205) (GPX1_BOVIN)search Bos taurussearch 97% 198 93%
B GLUTATHIONE PEROXIDASE P00435 (8-205) (GPX1_BOVIN)search Bos taurussearch 97% 198 93%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00435 (8 - 205) GLUTATHIONE PEROXIDASE Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P00435) Glutathione peroxidase-likesearch Glutaredoxinsearch PF00255: Glutathione peroxidasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P00435) glutathione peroxidase activitysearch peroxidase activitysearch oxidoreductase activitysearch oxidation-reduction processsearch response to oxidative stresssearch cytoplasmsearch

Chain InterPro annotation
A, B Glutathione peroxidasesearch Thioredoxin-like foldsearch Glutathione peroxidase conserved sitesearch