1HW8: Hmg-CoA reductase

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.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
4
Atoms
12,022
Mol. weight
202.57 kDa
Ligands
ADP, 114
Released
11 May 2001

Explore 1HW8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 18 helices, 19 β-strands

ElementResiduesLengthSheet
α-helix464-4718
α-helix488-50114
α-helix508-5114
β-strand52311
β-strand52711
β-strand530-546172
β-strand549-55682
α-helix562-57514
β-strand57912
β-strand580-58783
β-strand588-59034
β-strand593-59534
α-helix599-61012
α-helix612-62312
β-strand630-639104
β-strand642-65094
β-strand65115
β-strand65315
β-strand65416
α-helix657-67418
β-strand679-68244
α-helix695-7006
β-strand703-712103
α-helix714-7196
α-helix725-7317
α-helix732-7398
α-helix740-7423
β-strand748-74923
α-helix753-76311
α-helix768-7703
α-helix771-7744
β-strand777-78483
β-strand790-800113
β-strand80516
α-helix807-8104
α-helix812-8209
α-helix833-85927
Chain B: 19 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix464-4729
α-helix478-4803
α-helix481-4844
α-helix488-50013
β-strand52317
β-strand52717
β-strand530-546172
β-strand549-55682
α-helix562-57514
β-strand57912
β-strand580-58788
β-strand588-59039
β-strand593-59539
α-helix599-61012
α-helix612-62312
β-strand629-639119
β-strand642-651109
β-strand654110
α-helix657-67418
β-strand679-68249
α-helix695-7006
β-strand703-712108
α-helix714-7196
α-helix725-7317
α-helix732-7398
α-helix740-7423
β-strand748-74928
α-helix753-76311
α-helix768-7703
α-helix771-7744
β-strand777-78488
β-strand790-800118
β-strand805110
α-helix807-8104
α-helix812-8209
α-helix833-85927
Chain C: 17 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix489-50012
α-helix508-5114
β-strand523111
β-strand527111
β-strand530-5461712
β-strand549-556812
α-helix562-57514
β-strand579112
β-strand580-587813
β-strand588-590314
β-strand593-595314
α-helix599-60911
α-helix612-62312
β-strand630-6391014
β-strand642-650914
β-strand654115
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-strand805115
α-helix807-8104
α-helix812-8209
α-helix833-85927
Chain D: 17 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix489-50113
α-helix506-5116
β-strand530-5461712
β-strand549-556812
α-helix562-57514
β-strand579112
β-strand580-587816
β-strand588-590317
β-strand593-595317
α-helix599-60911
α-helix612-62312
β-strand630-6391017
β-strand642-650917
β-strand654118
α-helix657-67418
β-strand679-682417
α-helix695-7006
β-strand703-7121016
α-helix714-7196
α-helix725-7317
α-helix732-7398
α-helix740-7423
β-strand748-749216
α-helix753-76311
α-helix768-7703
α-helix771-7744
β-strand777-784816
β-strand790-8001116
β-strand805118
α-helix807-8104
α-helix812-8209
α-helix833-85826

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hmg-CoA reductaseA, B, C, Dprotein467Homo sapiensP04035 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1HW8_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 P22
114(3R,5R)-3,5-dihydroxy-7-[(1S,2S,8S,8aR)-2-methyl-8-{[(2S)-2-methylbutanoyl]oxy}…C23 H36 O64

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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