1wpq Summary

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Ternary Complex Of Glycerol 3-phosphate Dehydrogenase 1 with NAD and dihydroxyactone

The structure was published by Ou, X., Ji, C., Han, X., et al., Wong, L.L., Bartlam, M., and Rao, Z., in 2006 in a paper entitled "Crystal Structures of Human Glycerol 3-phosphate Dehydrogenase 1 (GPD1)" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2004.

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

This PDB entry contains multiple copies of the structure of Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic.

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 [NAD+], cytoplasmic P21695 (1-349) (GPDA_HUMAN)search Homo sapienssearch 100% 349 99%
B Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic P21695 (1-349) (GPDA_HUMAN)search Homo sapienssearch 100% 349 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P21695 (1 - 349) Glycerol-3-phosphate dehydrogenase [NAD+], cytoplasmic Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B (P21695) 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 Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (P21695) glycerol-3-phosphate dehydrogenase [NAD+] activitysearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch NAD bindingsearch protein homodimerization activitysearch coenzyme bindingsearch oxidoreductase activitysearch glycerol-3-phosphate dehydrogenase activitysearch glycerol-3-phosphate catabolic processsearch oxidation-reduction processsearch carbohydrate metabolic processsearch cellular lipid metabolic processsearch small molecule metabolic processsearch NADH metabolic processsearch gluconeogenesissearch phospholipid metabolic processsearch cellular response to tumor necrosis factorsearch triglyceride biosynthetic processsearch glycerophospholipid biosynthetic processsearch glycerol-3-phosphate metabolic processsearch glycerophosphate shuttlesearch positive regulation of glycolytic processsearch glycerolipid metabolic processsearch cellular response to cAMPsearch phosphatidic acid biosynthetic processsearch NADH oxidationsearch glycerol-3-phosphate dehydrogenase complexsearch cytoplasmsearch extracellular vesicular exosomesearch cytosolsearch mitochondrionsearch

Chain InterPro annotation
A, B 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 Glycerol-3-phosphate dehydrogenase, NAD-dependent, eukaryoticsearch