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Yorodumi- PDB-2aow: Histamine Methyltransferase (Natural Variant I105) Complexed with... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2aow | ||||||
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Title | Histamine Methyltransferase (Natural Variant I105) Complexed with the Acetylcholinesterase Inhibitor and Altzheimer's Disease Drug Tacrine | ||||||
Components | Histamine N-methyltransferase | ||||||
Keywords | TRANSFERASE / CLASSIC METHYLTRANSFERASE FOLD / PROTEIN-DRUG COMPLEX | ||||||
Function / homology | Function and homology information 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 / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.97 Å | ||||||
Authors | Horton, J.R. / Sawada, K. / Nishibori, M. / Cheng, X. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 Title: Structural basis for inhibition of histamine N-methyltransferase by diverse drugs Authors: Horton, J.R. / Sawada, K. / Nishibori, M. / Cheng, X. #1: Journal: Structure / Year: 2001 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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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2aow.cif.gz | 122.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2aow.ent.gz | 95.7 KB | Display | PDB format |
PDBx/mmJSON format | 2aow.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ao/2aow ftp://data.pdbj.org/pub/pdb/validation_reports/ao/2aow | HTTPS FTP |
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-Related structure data
Related structure data | 2aotC 2aouC 2aovC 2aoxC 1jqdS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-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: 33345.070 Da / Num. of mol.: 2 / Fragment: Histamine methyltransferase / Mutation: T105I Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HNMT / Plasmid: PGEX-4T-3 / Production host: Escherichia coli (E. coli) / Strain (production host): DH5A / References: UniProt: P50135, histamine N-methyltransferase #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.4 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 6000, MES, ethyleneglycol, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 173 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1.1 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 18, 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: 2.97→28 Å / Num. all: 13697 / Num. obs: 13697 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.4 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 13.1 |
Reflection shell | Resolution: 2.97→3.04 Å / Rmerge(I) obs: 0.213 / Num. unique all: 791 / % possible all: 98.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 1JQD Resolution: 2.97→28 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 39.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.97→28 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.97→3.04 Å / Rfactor Rfree error: 0.044 /
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