1evy Summary



The structure was published by Suresh, S., Turley, S., Opperdoes, F.R., Michels, P.A., and Hol, W.G., in 2000 in a paper entitled "A potential target enzyme for trypanocidal drugs revealed by the crystal structure of NAD-dependent glycerol-3-phosphate dehydrogenase from Leishmania mexicana." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.75 Å and deposited in 2000.

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

The PDB entry contains the structure of GLYCEROL-3-PHOSPHATE DEHYDROGENASE. This molecule has the UniProt identifier P90551 (GPDA_LEIME)search. The sample contained 366 residues which is 100% of the natural sequence. Out of 366 residues 345 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 GLYCEROL-3-PHOSPHATE DEHYDROGENASE P90551 (1-366) (GPDA_LEIME)search Leishmania mexicanasearch 100% 366 94%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P90551 (1 - 366) GLYCEROL-3-PHOSPHATE DEHYDROGENASE Leishmania mexicana

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P90551) Glycerol-3-phosphate dehydrogenasesearch, 6-phosphogluconate dehydrogenase-like, N-terminal domainsearch NAD(P)-binding Rossmann-like Domainsearch, N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase; domain 2search PF01210: NAD-dependent glycerol-3-phosphate dehydrogenase N-terminussearch, PF07479: NAD-dependent glycerol-3-phosphate dehydrogenase C-terminussearch

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A (P90551) oxidation-reduction processsearch carbohydrate metabolic processsearch glycerol-3-phosphate metabolic processsearch glycerol-3-phosphate catabolic processsearch glycosomesearch cytoplasmsearch glycerol-3-phosphate dehydrogenase complexsearch peroxisomesearch glycerol-3-phosphate dehydrogenase [NAD+] activitysearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch NAD bindingsearch coenzyme bindingsearch oxidoreductase activitysearch

Chain InterPro annotation
A Glycerol-3-phosphate dehydrogenase, NAD-dependent, C-terminalsearch Glycerol-3-phosphate dehydrogenase, NAD-dependentsearch 6-phosphogluconate dehydrogenase, C-terminal-likesearch Glycerol-3-phosphate dehydrogenase, NAD-dependent, N-terminalsearch Dehydrogenase, multihelicalsearch NAD(P)-binding domainsearch