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- PDB-1hwl: 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: 1hwl | ||||||
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Title | COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ROSUVASTATIN (FORMALLY KNOWN AS ZD4522) | ||||||
![]() | 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 | ![]() | 309.2 KB | Display | ![]() |
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PDB format | ![]() | 247.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.6 MB | Display | ![]() |
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Full document | ![]() | 2.6 MB | Display | |
Data in XML | ![]() | 58.9 KB | Display | |
Data in CIF | ![]() | 78.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1hw8C ![]() 1hw9C ![]() 1hwiC ![]() 1hwjC ![]() 1hwkC ![]() 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 | #3: Chemical | ChemComp-FBI / #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 |
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Diffraction source |
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Detector |
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Radiation | Monochromator: horizontally bent Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.1→100 Å / Num. all: 101858 / Num. obs: 101858 / % possible obs: 97.6 % / Observed criterion σ(I): -3 / Redundancy: 5 % / Biso Wilson estimate: 27.1 Å2 / Rmerge(I) obs: 0.072 / Net I/σ(I): 21.1 | |||||||||||||||
Reflection shell | Resolution: 2.1→2.14 Å / Redundancy: 2 % / Rmerge(I) obs: 0.473 / Mean I/σ(I) obs: 1.3 / Num. unique all: 4532 / % possible all: 87.6 | |||||||||||||||
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: 2.1→43.29 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 2376841.76 / 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: 32.16 Å2 / ksol: 0.353 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 55.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.1→43.29 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: 2.1→2.23 Å / Rfactor Rfree error: 0.017 / 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 % / Rfactor obs: 0.219 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 55.4 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.314 / % reflection Rfree: 2.1 % / Rfactor Rwork: 0.329 |