+Open data
-Basic information
Entry | Database: PDB / ID: 1gos | ||||||
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Title | Human Monoamine Oxidase B | ||||||
Components | MONOAMINE OXIDASE | ||||||
Keywords | OXIDOREDUCTASE / FAD-CONTAINING AMINE OXIDASE | ||||||
Function / homology | Function and homology information Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB / aliphatic amine oxidase activity / monoamine oxidase activity / monoamine oxidase / phenylethylamine catabolic process / positive regulation of dopamine metabolic process / primary amine oxidase activity / negative regulation of serotonin secretion / response to aluminum ion / response to selenium ion ...Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB / aliphatic amine oxidase activity / monoamine oxidase activity / monoamine oxidase / phenylethylamine catabolic process / positive regulation of dopamine metabolic process / primary amine oxidase activity / negative regulation of serotonin secretion / response to aluminum ion / response to selenium ion / : / dopamine catabolic process / primary-amine oxidase / 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 | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SIR / Resolution: 3 Å | ||||||
Authors | Binda, C. / Newton-Vinson, P. / Hubalek, F. / Edmondson, D.E. / Mattevi, A. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2001 Title: Structure of Human Monoamine Oxidase B, a Drug Target for the Treatment of Neurological Disorders Authors: Binda, C. / Newton-Vinson, P. / Hubalek, F. / Edmondson, D.E. / Mattevi, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gos.cif.gz | 201.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gos.ent.gz | 169.9 KB | Display | PDB format |
PDBx/mmJSON format | 1gos.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/go/1gos ftp://data.pdbj.org/pub/pdb/validation_reports/go/1gos | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.55753, -0.48823, -0.67142), Vector: |
-Components
#1: Protein | Mass: 58837.730 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: PICHIA PASTORIS (fungus) / References: UniProt: P27338, monoamine oxidase #2: Chemical | #3: Chemical | |
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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: 2.85 Å3/Da / Density % sol: 57 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.50 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.934 |
Detector | Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 3→40 Å / Num. obs: 24034 / % possible obs: 95.3 % / Redundancy: 8.1 % / Rmerge(I) obs: 0.128 |
Reflection shell | *PLUS % possible obs: 94.6 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.338 |
-Processing
Software |
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Refinement | Method to determine structure: SIR / Resolution: 3→40 Å
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Refinement step | Cycle: LAST / Resolution: 3→40 Å
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Refinement | *PLUS Lowest resolution: 40 Å / Rfactor obs: 0.23 / Rfactor Rwork: 0.23 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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