Complex of the catalytic portion of human hmg-CoA reductase with compactin (also known as mevastatin). Determined by X-ray diffraction at 2.1 Å resolution. Released 11 May 2001.
Explore 1HW8 in 3D Show helices and sheets RCSB PDB PDBe
1HW8 contains 71 α-helices and 68 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 464-471 | 8 | |
| α-helix | 488-501 | 14 | |
| α-helix | 508-511 | 4 | |
| β-strand | 523 | 1 | 1 |
| β-strand | 527 | 1 | 1 |
| β-strand | 530-546 | 17 | 2 |
| β-strand | 549-556 | 8 | 2 |
| α-helix | 562-575 | 14 | |
| β-strand | 579 | 1 | 2 |
| β-strand | 580-587 | 8 | 3 |
| β-strand | 588-590 | 3 | 4 |
| β-strand | 593-595 | 3 | 4 |
| α-helix | 599-610 | 12 | |
| α-helix | 612-623 | 12 | |
| β-strand | 630-639 | 10 | 4 |
| β-strand | 642-650 | 9 | 4 |
| β-strand | 651 | 1 | 5 |
| β-strand | 653 | 1 | 5 |
| β-strand | 654 | 1 | 6 |
| α-helix | 657-674 | 18 | |
| β-strand | 679-682 | 4 | 4 |
| α-helix | 695-700 | 6 | |
| β-strand | 703-712 | 10 | 3 |
| α-helix | 714-719 | 6 | |
| α-helix | 725-731 | 7 | |
| α-helix | 732-739 | 8 | |
| α-helix | 740-742 | 3 | |
| β-strand | 748-749 | 2 | 3 |
| α-helix | 753-763 | 11 | |
| α-helix | 768-770 | 3 | |
| α-helix | 771-774 | 4 | |
| β-strand | 777-784 | 8 | 3 |
| β-strand | 790-800 | 11 | 3 |
| β-strand | 805 | 1 | 6 |
| α-helix | 807-810 | 4 | |
| α-helix | 812-820 | 9 | |
| α-helix | 833-859 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 464-472 | 9 | |
| α-helix | 478-480 | 3 | |
| α-helix | 481-484 | 4 | |
| α-helix | 488-500 | 13 | |
| β-strand | 523 | 1 | 7 |
| β-strand | 527 | 1 | 7 |
| β-strand | 530-546 | 17 | 2 |
| β-strand | 549-556 | 8 | 2 |
| α-helix | 562-575 | 14 | |
| β-strand | 579 | 1 | 2 |
| β-strand | 580-587 | 8 | 8 |
| β-strand | 588-590 | 3 | 9 |
| β-strand | 593-595 | 3 | 9 |
| α-helix | 599-610 | 12 | |
| α-helix | 612-623 | 12 | |
| β-strand | 629-639 | 11 | 9 |
| β-strand | 642-651 | 10 | 9 |
| β-strand | 654 | 1 | 10 |
| α-helix | 657-674 | 18 | |
| β-strand | 679-682 | 4 | 9 |
| α-helix | 695-700 | 6 | |
| β-strand | 703-712 | 10 | 8 |
| α-helix | 714-719 | 6 | |
| α-helix | 725-731 | 7 | |
| α-helix | 732-739 | 8 | |
| α-helix | 740-742 | 3 | |
| β-strand | 748-749 | 2 | 8 |
| α-helix | 753-763 | 11 | |
| α-helix | 768-770 | 3 | |
| α-helix | 771-774 | 4 | |
| β-strand | 777-784 | 8 | 8 |
| β-strand | 790-800 | 11 | 8 |
| β-strand | 805 | 1 | 10 |
| α-helix | 807-810 | 4 | |
| α-helix | 812-820 | 9 | |
| α-helix | 833-859 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 489-500 | 12 | |
| α-helix | 508-511 | 4 | |
| β-strand | 523 | 1 | 11 |
| β-strand | 527 | 1 | 11 |
| β-strand | 530-546 | 17 | 12 |
| β-strand | 549-556 | 8 | 12 |
| α-helix | 562-575 | 14 | |
| β-strand | 579 | 1 | 12 |
| β-strand | 580-587 | 8 | 13 |
| β-strand | 588-590 | 3 | 14 |
| β-strand | 593-595 | 3 | 14 |
| α-helix | 599-609 | 11 | |
| α-helix | 612-623 | 12 | |
| β-strand | 630-639 | 10 | 14 |
| β-strand | 642-650 | 9 | 14 |
| β-strand | 654 | 1 | 15 |
| α-helix | 657-674 | 18 | |
| β-strand | 679-682 | 4 | 14 |
| α-helix | 695-700 | 6 | |
| β-strand | 703-712 | 10 | 13 |
| α-helix | 714-719 | 6 | |
| α-helix | 725-731 | 7 | |
| α-helix | 732-737 | 6 | |
| α-helix | 738-742 | 5 | |
| β-strand | 748-749 | 2 | 13 |
| α-helix | 753-763 | 11 | |
| α-helix | 768-770 | 3 | |
| α-helix | 771-774 | 4 | |
| β-strand | 777-784 | 8 | 13 |
| β-strand | 790-800 | 11 | 13 |
| β-strand | 805 | 1 | 15 |
| α-helix | 807-810 | 4 | |
| α-helix | 812-820 | 9 | |
| α-helix | 833-859 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 489-501 | 13 | |
| α-helix | 506-511 | 6 | |
| β-strand | 530-546 | 17 | 12 |
| β-strand | 549-556 | 8 | 12 |
| α-helix | 562-575 | 14 | |
| β-strand | 579 | 1 | 12 |
| β-strand | 580-587 | 8 | 16 |
| β-strand | 588-590 | 3 | 17 |
| β-strand | 593-595 | 3 | 17 |
| α-helix | 599-609 | 11 | |
| α-helix | 612-623 | 12 | |
| β-strand | 630-639 | 10 | 17 |
| β-strand | 642-650 | 9 | 17 |
| β-strand | 654 | 1 | 18 |
| α-helix | 657-674 | 18 | |
| β-strand | 679-682 | 4 | 17 |
| α-helix | 695-700 | 6 | |
| β-strand | 703-712 | 10 | 16 |
| α-helix | 714-719 | 6 | |
| α-helix | 725-731 | 7 | |
| α-helix | 732-739 | 8 | |
| α-helix | 740-742 | 3 | |
| β-strand | 748-749 | 2 | 16 |
| α-helix | 753-763 | 11 | |
| α-helix | 768-770 | 3 | |
| α-helix | 771-774 | 4 | |
| β-strand | 777-784 | 8 | 16 |
| β-strand | 790-800 | 11 | 16 |
| β-strand | 805 | 1 | 18 |
| α-helix | 807-810 | 4 | |
| α-helix | 812-820 | 9 | |
| α-helix | 833-858 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hmg-CoA reductase | A, B, C, D | protein | 467 | Homo sapiens | P04035 (AlphaFold model) |
>1HW8_1 HMG-COA REDUCTASE (chains A, B, C, D) GAMASSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKL ETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVA GPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACD SAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMIS KGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVL KTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLM EASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARI VCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
| 114 | (3R,5R)-3,5-dihydroxy-7-[(1S,2S,8S,8aR)-2-methyl-8-{[(2S)-2-methylbutanoyl]oxy}… | C23 H36 O6 | 4 |
Structural mechanism for statin inhibition of HMG-CoA reductase. Istvan, E.S., Deisenhofer, J. Science (2001) 292:1160-1164. DOI 10.1126/science.1059344 · PubMed
Other PDB entries of the same protein (UniProt P04035 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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