1ag8 Summary



The structure was published by Steinmetz, C.G., Xie, P., Weiner, H., and Hurley, T.D., in 1997 in a paper entitled "Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.65 Å and deposited in 1997.

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

This PDB entry contains multiple copies of the structure of ALDEHYDE DEHYDROGENASE.

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 ALDEHYDE DEHYDROGENASE P20000 (22-520) (ALDH2_BOVIN)search Bos taurussearch 96% 499 98%
B ALDEHYDE DEHYDROGENASE P20000 (22-520) (ALDH2_BOVIN)search Bos taurussearch 96% 499 98%
C ALDEHYDE DEHYDROGENASE P20000 (22-520) (ALDH2_BOVIN)search Bos taurussearch 96% 499 98%
D ALDEHYDE DEHYDROGENASE P20000 (22-520) (ALDH2_BOVIN)search Bos taurussearch 96% 499 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P20000 (22 - 520) ALDEHYDE DEHYDROGENASE Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P20000) ALDH-likesearch Aldehyde Dehydrogenase; Chain A, domain 1search, Aldehyde Dehydrogenase; Chain A, domain 2search PF00171: Aldehyde dehydrogenase familysearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B, C, D (P20000) mitochondrionsearch mitochondrial matrixsearch aldehyde dehydrogenase (NAD) activitysearch oxidoreductase activitysearch oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptorsearch ethanol catabolic processsearch metabolic processsearch oxidation-reduction processsearch

Chain InterPro annotation
A, B, C, D Aldehyde dehydrogenase domainsearch Aldehyde dehydrogenase, cysteine active sitesearch Aldehyde/histidinol dehydrogenasesearch Aldehyde dehydrogenase N-terminal domainsearch Aldehyde dehydrogenase, C-terminalsearch Aldehyde dehydrogenase, glutamic acid active sitesearch