1dhr Summary

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CRYSTAL STRUCTURE OF RAT LIVER DIHYDROPTERIDINE REDUCTASE

The structure was published by Varughese, K.I., Skinner, M.M., Whiteley, J.M., Matthews, D.A., and Xuong, N.H., in 1992 in a paper entitled "Crystal structure of rat liver dihydropteridine reductase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1992.

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

The PDB entry contains the structure of DIHYDROPTERIDINE REDUCTASE. This molecule has the UniProt identifier P11348 (DHPR_RAT)search. The sample contained 241 residues which is 100% of the natural sequence. Out of 241 residues 236 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 DIHYDROPTERIDINE REDUCTASE P11348 (1-241) (DHPR_RAT)search Rattus norvegicussearch 100% 241 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P11348 (1 - 241) DIHYDROPTERIDINE REDUCTASE Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P11348) Tyrosine-dependent oxidoreductasessearch NAD(P)-binding Rossmann-like Domainsearch PF00106: short chain dehydrogenasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P11348) tetrahydrobiopterin biosynthetic processsearch L-phenylalanine catabolic processsearch liver developmentsearch cellular response to drugsearch response to lead ionsearch metabolic processsearch response to aluminum ionsearch oxidation-reduction processsearch response to glucagonsearch NADPH bindingsearch 6,7-dihydropteridine reductase activitysearch oxidoreductase activitysearch NADH bindingsearch protein homodimerization activitysearch cytosolsearch mitochondrionsearch extracellular vesicular exosomesearch neuron projectionsearch cytoplasmsearch

Chain InterPro annotation
A Short-chain dehydrogenase/reductase SDRsearch NAD(P)-binding domainsearch Short-chain dehydrogenase/reductase, conserved sitesearch