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- PDB-2aou: Histamine Methyltransferase Complexed with the Antimalarial Drug ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2aou | ||||||
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Title | Histamine Methyltransferase Complexed with the Antimalarial Drug Amodiaquine | ||||||
![]() | (Histamine N-methyltransferase) x 2 | ||||||
![]() | TRANSFERASE / CLASSIC METHYLTRANSFERASE FOLD / PROTEIN-DRUG COMPLEX | ||||||
Function / homology | ![]() histamine N-methyltransferase / histamine catabolic process / histamine N-methyltransferase activity / histamine metabolic process / Histidine catabolism / L-histidine catabolic process / Metabolism of ingested SeMet, Sec, MeSec into H2Se / respiratory gaseous exchange by respiratory system / methylation / centrosome ...histamine N-methyltransferase / histamine catabolic process / histamine N-methyltransferase activity / histamine metabolic process / Histidine catabolism / L-histidine catabolic process / Metabolism of ingested SeMet, Sec, MeSec into H2Se / respiratory gaseous exchange by respiratory system / methylation / centrosome / extracellular exosome / nucleoplasm / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Horton, J.R. / Sawada, K. / Nishibori, M. / Cheng, X. | ||||||
![]() | ![]() Title: Structural basis for inhibition of histamine N-methyltransferase by diverse drugs Authors: Horton, J.R. / Sawada, K. / Nishibori, M. / Cheng, X. #1: ![]() Title: Polymorphic Forms of Human Histamine Methyltransferase: Structural, Thermal, and Kinetic Comparisons Authors: Horton, J.R. / Sawada, K. / Nishibori, M. / Zhang, X. / Cheng, X. | ||||||
History |
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Remark 600 | HETEROGEN Any one of the three ethyl groups on ligand, CQA 400 could be the alternative ...HETEROGEN Any one of the three ethyl groups on ligand, CQA 400 could be the alternative conformation of the other two (by the rotation of approximately 120 or 240 drgrees). |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 135.6 KB | Display | ![]() |
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PDB format | ![]() | 104.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 701.9 KB | Display | ![]() |
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Full document | ![]() | 722.7 KB | Display | |
Data in XML | ![]() | 15.8 KB | Display | |
Data in CIF | ![]() | 24.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2aotC ![]() 2aovC ![]() 2aowC ![]() 2aoxC ![]() 1jqdS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 33349.020 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Protein | Mass: 33349.020 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
#3: Chemical | ChemComp-CQA / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.92 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.2 Details: PEG 6000, MES, ethyleneglycol, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 173 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jun 23, 2000 |
Radiation | Monochromator: SI(111) DOUBLE-CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. all: 27645 / Num. obs: 26928 / % possible obs: 97.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Biso Wilson estimate: 22.2 Å2 / Rmerge(I) obs: 0.076 / Net I/σ(I): 12.3 |
Reflection shell | Resolution: 2.3→2.35 Å / % possible all: 96.2 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1JQD Resolution: 2.3→30 Å / Isotropic thermal model: ANISOTROPIC / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 34.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.35 Å / Rfactor Rfree error: 0.024 /
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