1HWJ: Hmg-CoA reductase

Complex of the catalytic portion of human hmg-CoA reductase with cerivastatin. Determined by X-ray diffraction at 2.26 Å resolution. Released 11 May 2001.

Method
X-ray diffraction
Resolution
2.26 Å
Organism
Homo sapiens
Chains
4
Atoms
12,418
Mol. weight
204.5 kDa
Ligands
ADP, 116
Released
11 May 2001

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

Secondary structure: helices and β-sheets

1HWJ contains 79 α-helices and 74 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: 20 helices, 17 β-strands

ElementResiduesLengthSheet
α-helix447-4493
α-helix464-47310
α-helix478-4836
α-helix489-50113
α-helix519-5213
β-strand530-546171
β-strand549-55681
α-helix562-57514
β-strand57911
β-strand580-58782
β-strand588-59033
β-strand593-59533
α-helix599-60911
α-helix612-62312
β-strand630-639103
β-strand642-65093
β-strand65114
β-strand65314
β-strand65415
α-helix657-67418
β-strand679-68243
α-helix695-7006
β-strand703-712102
α-helix714-7196
α-helix725-7317
α-helix732-7376
α-helix738-7425
β-strand748-74922
α-helix753-76311
α-helix768-7703
α-helix771-7744
β-strand777-78482
β-strand790-800112
β-strand80515
α-helix807-8104
α-helix812-82110
α-helix833-85927
Chain B: 20 helices, 19 β-strands
ElementResiduesLengthSheet
α-helix464-4729
α-helix478-4803
α-helix481-4844
α-helix488-50013
α-helix508-5114
β-strand52316
β-strand52716
β-strand530-546171
β-strand549-55681
α-helix562-57413
β-strand57911
β-strand580-58787
β-strand588-59038
β-strand593-59538
α-helix599-61012
α-helix612-62312
β-strand630-639108
β-strand642-65098
β-strand65119
β-strand65319
β-strand654110
α-helix657-67418
β-strand679-68248
α-helix695-7006
β-strand703-712107
α-helix714-7196
α-helix725-7317
α-helix732-7398
α-helix740-7423
β-strand748-74927
α-helix753-76311
α-helix768-7703
α-helix771-7744
β-strand777-78487
β-strand790-800117
β-strand805110
α-helix807-8104
α-helix812-8209
α-helix833-85927
Chain C: 21 helices, 19 β-strands
ElementResiduesLengthSheet
α-helix464-47411
α-helix478-4803
α-helix481-4844
α-helix489-50012
α-helix508-5114
α-helix519-5224
β-strand523111
β-strand527111
β-strand530-5461712
β-strand549-556812
α-helix562-57413
β-strand579112
β-strand580-587813
β-strand588-590314
β-strand593-595314
α-helix599-60911
α-helix612-62312
β-strand630-6391014
β-strand642-650914
β-strand651115
β-strand653115
β-strand654116
α-helix657-67418
β-strand679-682414
α-helix695-7006
β-strand703-7121013
α-helix714-7196
α-helix725-7317
α-helix732-7376
α-helix738-7425
β-strand748-749213
α-helix753-76311
α-helix768-7703
α-helix771-7744
β-strand777-784813
β-strand790-8001113
β-strand805116
α-helix807-8104
α-helix812-8209
α-helix833-85927
Chain D: 18 helices, 19 β-strands
ElementResiduesLengthSheet
α-helix464-4729
α-helix488-50013
α-helix506-5116
β-strand523117
β-strand527117
β-strand530-5461712
β-strand549-556812
α-helix562-57514
β-strand579112
β-strand580-587818
β-strand588-590319
β-strand593-595319
α-helix599-60911
α-helix612-62312
β-strand630-6391019
β-strand642-650919
β-strand651120
β-strand653120
β-strand654121
α-helix657-67418
β-strand679-682419
α-helix695-7006
β-strand703-7121018
α-helix714-7196
α-helix725-7317
α-helix732-7398
α-helix740-7423
β-strand748-749218
α-helix753-76311
α-helix768-7703
α-helix771-7744
β-strand777-784818
β-strand790-8001118
β-strand805121
α-helix807-8104
α-helix812-8209
α-helix833-85927

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hmg-CoA reductaseA, B, C, Dprotein467Homo sapiensP04035 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1HWJ_1 HMG-COA REDUCTASE (chains A, B, C, D)
GAMASSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKL
ETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVA
GPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACD
SAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMIS
KGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVL
KTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLM
EASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARI
VCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P26
1167-[4-(4-fluoro-phenyl)-5-hydroxymethyl-2,6-diisopropyl-pyridin-3-yl]-3,5-dihydr…C26 H36 F N O54

Primary citation

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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