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- PDB-1hwk: COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hwk | ||||||
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Title | COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ATORVASTATIN | ||||||
![]() | HMG-COA REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / protein-inhibitor complex | ||||||
Function / homology | ![]() hydroxymethylglutaryl-CoA reductase (NADPH) / hydroxymethylglutaryl-CoA reductase (NADPH) activity / sterol biosynthetic process / GTPase regulator activity / coenzyme A binding / negative regulation of amyloid-beta clearance / Cholesterol biosynthesis / EGR2 and SOX10-mediated initiation of Schwann cell myelination / coenzyme A metabolic process / ergosterol biosynthetic process ...hydroxymethylglutaryl-CoA reductase (NADPH) / hydroxymethylglutaryl-CoA reductase (NADPH) activity / sterol biosynthetic process / GTPase regulator activity / coenzyme A binding / negative regulation of amyloid-beta clearance / Cholesterol biosynthesis / EGR2 and SOX10-mediated initiation of Schwann cell myelination / coenzyme A metabolic process / ergosterol biosynthetic process / isoprenoid biosynthetic process / peroxisomal membrane / cholesterol biosynthetic process / negative regulation of protein secretion / NADPH binding / regulation of ERK1 and ERK2 cascade / Activation of gene expression by SREBF (SREBP) / long-term synaptic potentiation / visual learning / negative regulation of protein catabolic process / PPARA activates gene expression / endoplasmic reticulum membrane / endoplasmic reticulum Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Istvan, E.S. / Deisenhofer, J. | ||||||
![]() | ![]() Title: Structural mechanism for statin inhibition of HMG-CoA reductase. Authors: Istvan, E.S. / Deisenhofer, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 313.5 KB | Display | ![]() |
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PDB format | ![]() | 251.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.2 MB | Display | ![]() |
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Full document | ![]() | 3.2 MB | Display | |
Data in XML | ![]() | 58.8 KB | Display | |
Data in CIF | ![]() | 79.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1hw8C ![]() 1hw9C ![]() 1hwiC ![]() 1hwjC ![]() 1hwlC ![]() 1dqaS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 50021.523 Da / Num. of mol.: 4 / Fragment: CATALYTIC PORTION / Mutation: M485I Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P04035, hydroxymethylglutaryl-CoA reductase (NADPH) #2: Chemical | ChemComp-ADP / #3: Chemical | ChemComp-117 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 294 K / Method: microseeding / pH: 7.5 Details: PEG 4000, ammonium acetate, glycerol, DTT, Hepes, Microseeding, pH 7.5 at 294 K, microseeding | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ / Method: batch method / Details: used microseeding | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 123 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 1, 2000 / Details: mirror |
Radiation | Monochromator: horizontally bent Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.942 Å / Relative weight: 1 |
Reflection | Resolution: 2.21→100 Å / Num. all: 87343 / Num. obs: 87343 / % possible obs: 98.6 % / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Biso Wilson estimate: 32.8 Å2 / Rmerge(I) obs: 0.038 / Net I/σ(I): 30.8 |
Reflection shell | Resolution: 2.21→2.25 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.309 / Mean I/σ(I) obs: 3.3 / Num. unique all: 3712 / % possible all: 84.3 |
Reflection | *PLUS |
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Processing
Software |
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Refinement | Method to determine structure: difference fourier Starting model: pdb entry 1dqa Resolution: 2.22→43.4 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 2363054.06 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(I): -3 / Stereochemistry target values: Engh & Huber / Details: ncs-restraints were used
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 31.21 Å2 / ksol: 0.346 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 52.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.22→43.4 Å
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Refine LS restraints |
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Refine LS restraints NCS | Weight Biso : 5 / Weight position: 250 | ||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.22→2.36 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS % reflection Rfree: 2.3 % / Rfactor obs: 0.212 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 52.7 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.366 / % reflection Rfree: 2.4 % / Rfactor Rwork: 0.325 |