3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR) is a 888-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P04035.
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The mean pLDDT of this model is 75.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 45% |
| 70 to 90 | Confident: backbone generally right | 18% |
| 50 to 70 | Low: treat with caution | 17% |
| Below 50 | Very low: often disordered regions | 21% |
What pLDDT means and how to read it
Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis (PubMed:21357570, PubMed:2991281, PubMed:36745799, PubMed:6995544). HMGCR is the main target of statins, a class of cholesterol-lowering drugs (PubMed:11349148, PubMed:18540668, PubMed:36745799)
Homotetramer (PubMed:10698924). Homodimer (PubMed:10698924). Interacts (via its SSD) with INSIG1; the interaction, accelerated by sterols, leads to the recruitment of HMGCR to AMFR/gp78 for its ubiquitination by the sterol-mediated ERAD pathway (PubMed:12535518, PubMed:19458199). Interacts with UBIAD1 (PubMed:23169578)
Endoplasmic reticulum membrane, Peroxisome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 2R4F | X-ray | 1.7 Å | A/B/C/D=441-875 |
| 3CCZ | X-ray | 1.7 Å | A/B/C/D=441-875 |
| 1DQA | X-ray | 2.0 Å | A/B/C/D=425-888 |
| 2Q6B | X-ray | 2.0 Å | A/B/C/D=441-875 |
| 2Q6C | X-ray | 2.0 Å | A/B/C/D=441-875 |
| 2Q1L | X-ray | 2.05 Å | A/B/C/D=441-875 |
| 3CD7 | X-ray | 2.05 Å | A/B/C/D=441-875 |
| 8S6B | EM | 2.06 Å | A=439-861 |
| 3CDA | X-ray | 2.07 Å | A/B/C/D=441-875 |
| 1DQ8 | X-ray | 2.1 Å | A/B/C/D=425-888 |
| 1HW8 | X-ray | 2.1 Å | A/B/C/D=426-888 |
| 1HWL | X-ray | 2.1 Å | A/B/C/D=426-888 |
| 3CCW | X-ray | 2.1 Å | A/B/C/D=441-875 |
| 3CCT | X-ray | 2.12 Å | A/B/C/D=441-875 |
| 1HWK | X-ray | 2.22 Å | A/B/C/D=426-888 |
| 3BGL | X-ray | 2.23 Å | A/B/C/D=441-875 |
| 1HWJ | X-ray | 2.26 Å | A/B/C/D=426-888 |
| 8PKN | EM | 2.26 Å | A=439-861 |
| 1HWI | X-ray | 2.3 Å | A/B/C/D=426-888 |
| 3CDB | X-ray | 2.3 Å | A/B/C/D=441-875 |
Showing 20 of 24 experimental structures (best resolution first).
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