- PDB-3zyx: Crystal structure of human monoamine oxidase B in complex with me... -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 3zyx
Title
Crystal structure of human monoamine oxidase B in complex with methylene blue and bearing the double mutation I199A-Y326A
Components
AMINE OXIDASE [FLAVIN-CONTAINING] B
Keywords
OXIDOREDUCTASE / INHIBITOR
Function / homology
Function and homology information
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
Mass: 18.015 Da / Num. of mol.: 350 / Source method: isolated from a natural source / Formula: H2O
Compound details
ENGINEERED RESIDUE IN CHAIN A, ILE 199 TO ALA ENGINEERED RESIDUE IN CHAIN A, TYR 326 TO ALA ...ENGINEERED RESIDUE IN CHAIN A, ILE 199 TO ALA ENGINEERED RESIDUE IN CHAIN A, TYR 326 TO ALA ENGINEERED RESIDUE IN CHAIN B, ILE 199 TO ALA ENGINEERED RESIDUE IN CHAIN B, TYR 326 TO ALA
Sequence details
DISCREPANCIES OCCUR AT SITES 199 AND 326 BECAUSE SITE- DIRECTED MUTAGENESIS HAS BEEN PERFORMED IN ...DISCREPANCIES OCCUR AT SITES 199 AND 326 BECAUSE SITE- DIRECTED MUTAGENESIS HAS BEEN PERFORMED IN ORDER TO STUDY THESE GATING RESIDUES
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.74 Å3/Da / Density % sol: 52 % / Description: NONE
Crystal grow
pH: 6.5 Details: 12% PEG4000, 100 MM ADA PH 6.5, 70 MM LITHIUM SULPHATE, 8.5 MM ZWITTERGENT 3-12
Resolution: 2.2→43.31 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.882 / SU B: 5.036 / SU ML: 0.131 / Cross valid method: THROUGHOUT / ESU R: 0.229 / ESU R Free: 0.2 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.24401
1667
2.6 %
RANDOM
Rwork
0.19042
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obs
0.19179
62656
97.94 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK