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Yorodumi- PDB-2an5: Structure of human PNMT complexed with S-adenosyl-homocysteine an... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2an5 | ||||||
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Title | Structure of human PNMT complexed with S-adenosyl-homocysteine and an inhibitor, trans-(1S,2S)-2-amino-1-tetralol | ||||||
Components | Phenylethanolamine N-methyltransferase | ||||||
Keywords | TRANSFERASE / methyltransferase / inhibitor structure / S-adenosyl-L-methionine / adrenaline synthesis | ||||||
Function / homology | Function and homology information phenylethanolamine N-methyltransferase / phenylethanolamine N-methyltransferase activity / epinephrine biosynthetic process / Catecholamine biosynthesis / catecholamine biosynthetic process / methylation / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / FOURIER SYNTHESIS / Resolution: 2.5 Å | ||||||
Authors | Gee, C.L. / Tyndall, J.D.A. / Grunewald, G.L. / Wu, Q. / McLeish, M.J. / Martin, J.L. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Mode of binding of methyl acceptor substrates to the adrenaline-synthesizing enzyme phenylethanolamine N-methyltransferase: implications for catalysis Authors: Gee, C.L. / Tyndall, J.D.A. / Grunewald, G.L. / Wu, Q. / McLeish, M.J. / Martin, J.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2an5.cif.gz | 122.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2an5.ent.gz | 94.5 KB | Display | PDB format |
PDBx/mmJSON format | 2an5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2an5_validation.pdf.gz | 974.4 KB | Display | wwPDB validaton report |
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Full document | 2an5_full_validation.pdf.gz | 981.4 KB | Display | |
Data in XML | 2an5_validation.xml.gz | 23.3 KB | Display | |
Data in CIF | 2an5_validation.cif.gz | 32.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/an/2an5 ftp://data.pdbj.org/pub/pdb/validation_reports/an/2an5 | HTTPS FTP |
-Related structure data
Related structure data | 2an3C 2an4C 1hnnS 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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Details | enzyme is active as a monomer |
-Components
#1: Protein | Mass: 31845.967 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PNMT / Plasmid: pET17PNMT-his / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS References: UniProt: P11086, phenylethanolamine N-methyltransferase #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-PO4 / | #5: 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: 3.1 Å3/Da / Density % sol: 60.6 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 6000, LiCl, cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-E / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Sep 15, 2004 / Details: Osmic mirrors (HiRes2) |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→38.36 Å / Num. all: 29896 / Num. obs: 29890 / % possible obs: 100 % / Redundancy: 7.82 % / Rmerge(I) obs: 0.076 / Χ2: 1 / Net I/σ(I): 13.9 / Scaling rejects: 1766 |
Reflection shell | Resolution: 2.5→2.59 Å / % possible obs: 100 % / Redundancy: 7.87 % / Rmerge(I) obs: 0.462 / Mean I/σ(I) obs: 4.1 / Num. measured obs: 0 / Num. unique all: 2912 / Rsym value: 0 / Χ2: 1.22 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: PDB structure 1HNN Resolution: 2.5→38.36 Å / Rfactor Rfree error: 0.005 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 32.039 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 56.226 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→38.36 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.59 Å / Rfactor Rfree error: 0.023 / Total num. of bins used: 10
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Xplor file |
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