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- PDB-2bxr: Human Monoamine Oxidase A in complex with Clorgyline, Crystal Form A -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bxr | ||||||
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Title | Human Monoamine Oxidase A in complex with Clorgyline, Crystal Form A | ||||||
![]() | AMINE OXIDASE [FLAVIN-CONTAINING] A | ||||||
![]() | OXIDOREDUCTASE / NEUROTRANSMITTER / MEMBRANE-PROTEIN / FLAVIN | ||||||
Function / homology | ![]() Defective MAOA causes BRUNS / Dopamine clearance from the synaptic cleft / biogenic amine metabolic process / Enzymatic degradation of dopamine by COMT / Enzymatic degradation of Dopamine by monoamine oxidase / Metabolism of serotonin / Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB / monoamine oxidase activity / monoamine oxidase / positive regulation of signal transduction ...Defective MAOA causes BRUNS / Dopamine clearance from the synaptic cleft / biogenic amine metabolic process / Enzymatic degradation of dopamine by COMT / Enzymatic degradation of Dopamine by monoamine oxidase / Metabolism of serotonin / Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB / monoamine oxidase activity / monoamine oxidase / positive regulation of signal transduction / Norepinephrine Neurotransmitter Release Cycle / primary-amine oxidase / dopamine catabolic process / aliphatic amine oxidase activity / primary methylamine oxidase activity / flavin adenine dinucleotide binding / Interleukin-4 and Interleukin-13 signaling / mitochondrial outer membrane / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | De Colibus, L. / Binda, C. / Edmondson, D.E. / Mattevi, A. | ||||||
![]() | ![]() Title: Three-Dimensional Structure of Human Monoamine Oxidase a (Mao A): Relation to the Structures of Rat Mao a and Human Mao B Authors: De Colibus, L. / Li, M. / Binda, C. / Lustig, A. / Edmondson, D.E. / Mattevi, A. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 187.8 KB | Display | ![]() |
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PDB format | ![]() | 146.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 37.1 KB | Display | |
Data in CIF | ![]() | 48.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2bxsC ![]() 2bybC ![]() 1s2qS 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1
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Components
#1: Protein | Mass: 59759.504 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | #3: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.66 Å3/Da / Density % sol: 45 % |
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Crystal grow | pH: 6.5 Details: PROTEIN WAS CRYSTALLIZED FROM 6% PEG 6000, 100 MM LISULPHATE, 100 MM NACITRATE, 50 MM KPI PH 7.0. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Feb 14, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→15 Å / Num. obs: 23085 / % possible obs: 96.9 % / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Rmerge(I) obs: 0.01 |
Reflection shell | Resolution: 3→3.1 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.52 / % possible all: 97.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1S2Q Resolution: 3→87.04 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.917 / SU B: 37.83 / SU ML: 0.306 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.411 Stereochemistry target values: MAXIMUM LIKELIHOODWITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 63.9 Å2
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Refinement step | Cycle: LAST / Resolution: 3→87.04 Å
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Refine LS restraints |
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