1bg6 Summary

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CRYSTAL STRUCTURE OF THE N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE FROM ARTHROBACTER SP. STRAIN 1C

The structure was published by Britton, K.L., Asano, Y., and Rice, D.W., in 1998 in a paper entitled "Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1998.

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

The PDB entry contains the structure of N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE. This molecule has the UniProt identifier Q44297 (ODH_ARTSC)search. The sample contained 359 residues which is 100% of the natural sequence. Out of 359 residues 349 were observed and are deposited in the PDB.

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 N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE Q44297 (1-359) (ODH_ARTSC)search Arthrobacter sp. 1Csearch 100% 359 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q44297 (1 - 359) N-(1-D-CARBOXYLETHYL)-L-NORVALINE DEHYDROGENASE Arthrobacter sp. 1C

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q44297) N-(1-D-carboxylethyl)-L-norvaline 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, PF02317: NAD/NADP octopine/nopaline dehydrogenase, alpha-helical domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (Q44297) glycerol-3-phosphate catabolic processsearch oxidation-reduction processsearch opine dehydrogenase activitysearch NAD bindingsearch oxidoreductase activitysearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch coenzyme bindingsearch cytoplasmsearch

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