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- PDB-2xfo: tranylcypromine-inhibited human monoamine oxidase B Ile199Ala mut... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xfo | ||||||
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Title | tranylcypromine-inhibited human monoamine oxidase B Ile199Ala mutant in complex with 2-(2-benzofuranyl)-2-imidazoline | ||||||
![]() | Amine oxidase [flavin-containing] B | ||||||
![]() | OXIDOREDUCTASE / FLAVOPROTEIN | ||||||
Function / homology | ![]() Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB / monoamine oxidase activity / monoamine oxidase / phenylethylamine catabolic process / positive regulation of dopamine metabolic process / response to aluminum ion / negative regulation of serotonin secretion / response to selenium ion / primary-amine oxidase / dopamine catabolic process ...Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB / monoamine oxidase activity / monoamine oxidase / phenylethylamine catabolic process / positive regulation of dopamine metabolic process / response to aluminum ion / negative regulation of serotonin secretion / response to selenium ion / primary-amine oxidase / dopamine catabolic process / aliphatic amine oxidase activity / primary methylamine oxidase activity / mitochondrial envelope / hydrogen peroxide biosynthetic process / response to corticosterone / substantia nigra development / response to toxic substance / flavin adenine dinucleotide binding / response to ethanol / mitochondrial outer membrane / response to lipopolysaccharide / electron transfer activity / response to xenobiotic stimulus / neuronal cell body / dendrite / mitochondrion / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bonivento, D. / Milczek, E.M. / McDonald, G.R. / Binda, C. / Holt, A. / Edmondson, D.E. / Mattevi, A. | ||||||
![]() | ![]() Title: Potentiation of ligand binding through cooperative effects in monoamine oxidase B. Authors: Bonivento, D. / Milczek, E.M. / McDonald, G.R. / Binda, C. / Holt, A. / Edmondson, D.E. / Mattevi, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 217.8 KB | Display | ![]() |
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PDB format | ![]() | 173.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 979.8 KB | Display | ![]() |
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Full document | ![]() | 994.8 KB | Display | |
Data in XML | ![]() | 40.6 KB | Display | |
Data in CIF | ![]() | 57 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xcgC ![]() 2xfnC ![]() 2xfpC ![]() 2xfqC ![]() 2xfuC ![]() 1ojb C: citing same article ( S: Starting model for refinement |
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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
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 58795.652 Da / Num. of mol.: 2 / Mutation: 199A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 5 types, 309 molecules ![](data/chem/img/FA8.gif)
![](data/chem/img/3PL.gif)
![](data/chem/img/XCG.gif)
![](data/chem/img/FAD.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/3PL.gif)
![](data/chem/img/XCG.gif)
![](data/chem/img/FAD.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-FA8 / [[( | ||||||
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#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-FAD / | #6: Water | ChemComp-HOH / | |
-Details
Compound details | ENGINEEREDNonpolymer details | TRANYLCYPROMINE (TRA): CAK ATOM OF TRA IS COVALENTLY ATTACHED TO C4A ATOM OF FAD FLAVIN-ADENINE ...TRANYLCYPR | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.78 % / Description: NONE |
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Crystal grow | pH: 6.5 / Details: pH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. obs: 69410 / % possible obs: 95.5 % / Observed criterion σ(I): 1 / Redundancy: 2.9 % / Rmerge(I) obs: 0.02 / Net I/σ(I): 5.4 |
Reflection shell | Resolution: 2.1→2.21 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.581 / Mean I/σ(I) obs: 1.8 / % possible all: 97.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1OJB ![]() 1ojb Resolution: 2.1→65.27 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Refinement step | Cycle: LAST / Resolution: 2.1→65.27 Å
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