1teh Summary

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STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)

The structure was published by Yang, Z.N., Bosron, W.F., and Hurley, T.D., in 1997 in a paper entitled "Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 1996.

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

This PDB entry contains multiple copies of the structure of HUMAN CHICHI ALCOHOL DEHYDROGENASE.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 HUMAN CHICHI ALCOHOL DEHYDROGENASE P11766 (2-374) (ADHX_HUMAN)search Homo sapienssearch 100% 373 100%
B HUMAN CHICHI ALCOHOL DEHYDROGENASE P11766 (2-374) (ADHX_HUMAN)search Homo sapienssearch 100% 373 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P11766 (2 - 374) HUMAN CHICHI ALCOHOL DEHYDROGENASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P11766) Alcohol dehydrogenase-like, N-terminal domainsearch, Alcohol dehydrogenase-like, C-terminal domainsearch Medium-chain alcohol dehydrogenases, catalytic domainsearch, NAD(P)-binding Rossmann-like Domainsearch PF00107: Zinc-binding dehydrogenasesearch, PF08240: Alcohol dehydrogenase GroES-like domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B (P11766) oxidation-reduction processsearch ethanol oxidationsearch ethanol catabolic processsearch response to lipopolysaccharidesearch response to redox statesearch respiratory system processsearch retinoid metabolic processsearch positive regulation of blood pressuresearch peptidyl-cysteine S-nitrosylationsearch agingsearch formaldehyde catabolic processsearch response to nitrosative stresssearch zinc ion bindingsearch oxidoreductase activitysearch protein homodimerization activitysearch S-(hydroxymethyl)glutathione dehydrogenase activitysearch fatty acid bindingsearch formaldehyde dehydrogenase activitysearch alcohol dehydrogenase (NAD) activitysearch metal ion bindingsearch electron carrier activitysearch extracellular vesicular exosomesearch cytoplasmsearch mitochondrionsearch nucleussearch

Chain InterPro annotation
A, B Alcohol dehydrogenase superfamily, zinc-typesearch Alcohol dehydrogenase, zinc-type, conserved sitesearch GroES (chaperonin 10)-likesearch Alcohol dehydrogenase, C-terminalsearch Alcohol dehydrogenase GroES-likesearch Alcohol dehydrogenase class III/S-(hydroxymethyl)glutathione dehydrogenasesearch NAD(P)-binding domainsearch