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This page contains many different 3D-pictures of lysozyme structure. All these pictures are prepared with WebLab Viewer 4.0 with using coordinates of chicken egg-white lysozyme structure solved by X-Ray analysis at resolution 1.2 Angstrom.
Water molecules in all pictures of lysozyme structure were excluded from the final PDB file to make protein pictures more clearer. All these pictures, except residue conservation one, were made in the same orientation, which allow you to compare different mode of molecular representations.
For more clearer vision, all 3D pictures of lysozyme structure are accompanied with the stereo version. All stereo-pictures are made in relaxed eyes split screen mode with relative rotation of 3.5 degrees.
You can use these pictures for free for any non-commercial purpose, but you must refer to this web site (http://lysozyme.co.uk). For more details check copyright information.
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Pictures of Lysozyme structure
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Description
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Ball-and-stick representation
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Ball-and-stick representation of the lysozyme structure. In this view,
all protein atoms are shown as balls, and bonds between atoms are shown
as a stick. Carbon, nitrogen, oxygen and sulphur atoms are coloured grey,
blue, red and yellow, respectively. You also can check stereo-
representation of this picture here:
Structure of Lysozyme
ball-and-stick stereo picture.
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CPK representation
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CPK model of the lysozyme structure. In this view, all protein atoms
are shown as balls with size of approximately equal to van der Waals
radii. Carbon, nitrogen, oxygen and sulphur atoms are coloured grey,
blue, red and yellow, respectively. You also can check stereo-
representation of this picture here:
Structure of Lysozyme
CPK stereo picture.
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Van der Waals surface
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Van der Waal s surface of the lysozyme structure. In this view, the
smoothed surface of van der Waals radii is represented. Parts of the
surface corresponded to the carbon, nitrogen, oxygen and sulphur atoms
are coloured grey, blue, red and yellow, respectively. You also can
check stereo-representation of this picture here:
Structure of Lysozyme
van der Waals surface, stereo picture.
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Solvent-accessible surface
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Solvent accessible surface of the lysozyme structure. In this view, the
solvent-accessible surface is represented. Solvent-accessible surface
area was calculated by rolling ball method with a radius of 1.4 Angstrom
(
Lee, B. and Richards, F.M. (1971). The interpretation of protein structures:
estimation of static accesibility. J. Mol. Biol. 55,
379-400). Surface was colored in accordance with the electrostatic
potential of the surface, where positive potentials are drawn in blue
and red corresponds to the negative one. You also can check stereo-
representation of this picture here:
Structure of Lysozyme
Solvent accessible surface, stereo picture.
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Solid ribbon representation
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The main chain of lysozyme structure is represented in schematic view -
solid ribbon representation. Alpha-helices are shown by red
colour; beta-strands are coloured blue and irregular loops are
shown by grey rope.
You also can see stereo-representation of this picture here:
Structure of Lysozyme
monomer solid ribbon representation, stereo picture.
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Schematic representation
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The main chain of lysozyme structure is represented in schematic view.
Alpha-helices are shown by red coloured cylinders; beta-strands are
shown by blue coloured arrows and irregular loops are shown by grey rope. You also can see stereo-representation of this picture here:
Structure of Lysozyme
monomer schematic representation, stereo picture.
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CPK coloured by residue conservatism
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The CPK model of lysozyme structure. All residues are coloured by they conservatism.
From dark blue for variable residues through white for average variable residues
to dark magenta for completely conserved residues.Please note, that for
this picture, the orientation of the Lysozyme molecule is different form
that used for all other pictures presented on this page.
You also can see stereo-representation of this picture here:
Structure of Lysozyme
monomer schematic representation, stereo picture.
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