1DQA: Protein

Complex of the catalytic portion of human hmg-CoA reductase with hmg, CoA, and NADP+. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 Mar 2000.

Method

X-ray diffraction

Resolution

2.0 Å

Organism

Homo sapiens

Chains

4

Atoms

12,909

Mol. weight

206.78 kDa

Ligands

COA, MAH, NAP

Released

8 Mar 2000

Explore 1DQA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DQA contains 85 α-helices and 60 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 22 helices, 15 β-strands

Molecules and chains

>1DQA_1 PROTEIN (HMG-COA REDUCTASE) (chains A, B, C, D)
GAMASSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKL
ETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVA
GPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACD
SAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMIS
KGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVL
KTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLM
EASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARI
VCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA

Ligands and cofactors

Primary citation

Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis. Istvan, E.S., Palnitkar, M., Buchanan, S.K. et al. EMBO J (2000) 19:819-830. DOI 10.1093/emboj/19.5.819 · PubMed

Related structures

Other PDB entries of the same protein (UniProt P04035 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 2R4F 1.7 Å, Substituted Pyrazoles as Hepatselective HMG-COA reductase inhibitors
• 3CCZ 1.7 Å, Thermodynamic and structure guided design of statin hmg-coa reductase inhibitors
• 2Q6B 2.0 Å, Design and synthesis of novel, conformationally restricted HMG-COA reductase inhibitors
• 2Q6C 2.0 Å, Design and synthesis of novel, conformationally restricted HMG-COA reductase inhibitors
• 2Q1L 2.05 Å, Design and Synthesis of Pyrrole-based, Hepatoselective HMG-CoA Reductase Inhibitors
• 3CD7 2.05 Å, Thermodynamic and structure guided design of statin hmg-coa reductase inhibitors
• 8S6B 2.06 Å, CryoEM structure of Apo form of catalytic domain of human HMG-CoA reductase
• 3CDA 2.07 Å, Thermodynamic and structure guided design of statin hmg-coa reductase inhibitors
• 1DQ8 2.1 Å, Complex of the catalytic portion of human hmg-CoA reductase with hmg and CoA
• 1HW8 2.1 Å, Complex of the catalytic portion of human hmg-CoA reductase with compactin (also known…
• 1HWL 2.1 Å, Complex of the catalytic portion of human hmg-CoA reductase with rosuvastatin (formally…
• 3CCW 2.1 Å, Thermodynamic and structure guided design of statin hmg-coa reductase inhibitors

Browse structure collections

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