4i6w Summary


3-hydroxy-3-methylglutaryl (HMG) Coenzyme-A reductase complexed with thiomevalonate

The structure was published by Steussy, C.N., Critchelow, C.J., Schmidt, T., et al., Burgner, J.W., Rodwell, V.W., and Stauffacher, C.V., in 2013 in a paper entitled "A Novel Role for Coenzyme A during Hydride Transfer in 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.66 Å and deposited in 2012.

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

This PDB entry contains multiple copies of the structure of 3-hydroxy-3-methylglutaryl-coenzyme A 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 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 3-hydroxy-3-methylglutaryl-coenzyme A reductase P13702 (1-428) (MVAA_PSEMV)search Pseudomonas mevaloniisearch 100% 428 87%
B 3-hydroxy-3-methylglutaryl-coenzyme A reductase Not available
Pseudomonas mevaloniisearch 100% 428 87%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P13702 (1 - 428) 3-hydroxy-3-methylglutaryl-coenzyme A reductase Pseudomonas mevalonii

Chain Sequence family (Pfam)
A, B (P13702) PF00368: Hydroxymethylglutaryl-coenzyme A reductasesearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P13702) coenzyme A metabolic processsearch oxidation-reduction processsearch coenzyme bindingsearch oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptorsearch hydroxymethylglutaryl-CoA reductase activitysearch hydroxymethylglutaryl-CoA reductase (NADPH) activitysearch oxidoreductase activitysearch

Chain InterPro annotation
A, B Hydroxymethylglutaryl-CoA reductase, class I/IIsearch Hydroxymethylglutaryl-CoA reductase, bacterial-typesearch 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