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- PDB-3hce: Crystal Structure of E185D hPNMT in Complex With Octopamine and AdoHcy -
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Open data
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Basic information
Entry | Database: PDB / ID: 3hce | ||||||
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Title | Crystal Structure of E185D hPNMT in Complex With Octopamine and AdoHcy | ||||||
![]() | Phenylethanolamine N-methyltransferase | ||||||
![]() | TRANSFERASE / methyltransferase / Catecholamine biosynthesis / Polymorphism / S-adenosyl-L-methionine | ||||||
Function / homology | ![]() phenylethanolamine N-methyltransferase / phenylethanolamine N-methyltransferase activity / epinephrine biosynthetic process / Catecholamine biosynthesis / catecholamine biosynthetic process / methylation / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Drinkwater, N. / Martin, J.L. | ||||||
![]() | ![]() Title: Molecular recognition of physiological substrate noradrenaline by the adrenaline-synthesizing enzyme PNMT and factors influencing its methyltransferase activity. Authors: Drinkwater, N. / Gee, C.L. / Puri, M. / Criscione, K.R. / McLeish, M.J. / Grunewald, G.L. / Martin, J.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 224.4 KB | Display | ![]() |
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PDB format | ![]() | 181.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 946.4 KB | Display | ![]() |
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Full document | ![]() | 958 KB | Display | |
Data in XML | ![]() | 23.6 KB | Display | |
Data in CIF | ![]() | 31.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3hcaC ![]() 3hcbC ![]() 3hccC ![]() 3hcdC ![]() 3hcfC ![]() 1hnnS 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 31831.939 Da / Num. of mol.: 2 / Mutation: E185D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P11086, phenylethanolamine N-methyltransferase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.23 Å3/Da / Density % sol: 61.88 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.8 Details: PEG6K, LiCl, cacodylate, pH 5.8, vapor diffusion, hanging drop, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Aug 15, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95667 Å / Relative weight: 1 |
Reflection | Resolution: 2.85→50 Å / Num. obs: 20186 / Redundancy: 7.5 % / Biso Wilson estimate: 50.35 Å2 / Rmerge(I) obs: 0.098 / Net I/σ(I): 9.7 |
Reflection shell | Resolution: 2.85→2.9 Å / Redundancy: 6.6 % / Rmerge(I) obs: 0.833 / Mean I/σ(I) obs: 2.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1HNN Resolution: 2.85→45.445 Å / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.828 / SU ML: 0.37 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0.07 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 19.201 Å2 / ksol: 0.288 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 135.35 Å2 / Biso mean: 52.524 Å2 / Biso min: 14.27 Å2
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Refinement step | Cycle: LAST / Resolution: 2.85→45.445 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 12
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Refinement TLS params. | Method: refined / Origin x: 24.1876 Å / Origin y: 51.3494 Å / Origin z: -5.2075 Å
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Refinement TLS group |
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