1dqa Summary



The structure was published by Istvan, E.S., Palnitkar, M., Buchanan, S.K., and Deisenhofer, J., in 2000 in a paper entitled "Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1999.

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

This PDB entry contains multiple copies of the structure of PROTEIN (HMG-COA REDUCTASE).

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 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 PROTEIN (HMG-COA REDUCTASE) P04035 (426-888) (HMDH_HUMAN)search Homo sapienssearch < 90% 467 87%
B PROTEIN (HMG-COA REDUCTASE) P04035 (426-888) (HMDH_HUMAN)search Homo sapienssearch < 90% 467 87%
C PROTEIN (HMG-COA REDUCTASE) P04035 (426-888) (HMDH_HUMAN)search Homo sapienssearch < 90% 467 87%
D PROTEIN (HMG-COA REDUCTASE) P04035 (426-888) (HMDH_HUMAN)search Homo sapienssearch < 90% 467 87%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P04035 (426 - 888) PROTEIN (HMG-COA REDUCTASE) Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D NAD-binding domain of HMG-CoA reductasesearch, Substrate-binding domain of HMG-CoA reductasesearch HMGR, N-terminal domainsearch, 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2search, Alpha-Beta Plaitssearch Hydroxymethylglutaryl-coenzyme A reductasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B, C, D (P04035) isoprenoid biosynthetic processsearch oxidation-reduction processsearch coenzyme A metabolic processsearch hydroxymethylglutaryl-CoA reductase (NADPH) activitysearch NADP bindingsearch coenzyme bindingsearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch integral component of membranesearch endoplasmic reticulum membranesearch

Chain InterPro annotation
A, B, C, D Hydroxymethylglutaryl-CoA reductase, class I/IIsearch Hydroxymethylglutaryl-CoA reductase, eukaryotic/arcaheal typesearch Hydroxymethylglutaryl-CoA reductase, metazoansearch Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domainsearch Hydroxymethylglutaryl-CoA reductase, class I/II, substrate-binding domainsearch Hydroxymethylglutaryl-CoA reductase, class I/II, catalytic domainsearch Hydroxymethylglutaryl-CoA reductase, class I/II, conserved sitesearch Hydroxymethylglutaryl-CoA reductase, N-terminalsearch