Photosystem II structure
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| Photosystem II (view from the top; pdb: 1S5L.pdb) with it's Electron sidepath donors. The donors are CarD2 (red), Cytochome b559 (cyan) and the Chlorophyll Z2.
Distances are in Å. |
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| Photosystem II - la grande nation :) -
PSII (1S5L.pdb) core-structure with its cofactors. The subunits are D1 (blue), D2 (white) and Cytochrom b559 (red). The successive electron transfer steps are indicated.
Surface was generated by roling a 14Å sphere over the structure. |
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| Table with the distances between the cofactors in PSII (1S5L.pdb) in Å, pi to pi system. |
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| The water splitting part of PSII (1S5L.pdb) Tyrosin / His on the top, the Manganese (green) cluster with Calcium (cyan) and the µ oxo bridges glue them together (red). |
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| The water splitting part of PSII with two modelled waters instead of the bicarbonate. |
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Photosystem II structure comparison
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| psbA - the D1 protein with the main electron transfer cofactors. Backbone presentation with the colour coded displacement. |
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| psbB - the CP47 protein of photosystem II. Backbone presentation with the colour coded displacement. |
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| psbB - the CP43 protein of photosystem II. Backbone presentation with the colour coded displacement. |
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| Cytochome beta subunit (view from the side). Cpk illustration. |
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| psbA - the D2 protein with the main electron transfer cofactors. Backbone presentation with the colour coded displacement. |
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| Cytochome alpha subunit (view from the side). Backbone illustration. |
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| Cytochome alpha subunit (view from the side). Cpk illustration. |
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| Cytochome beta subunit (view from the side). Backbone illustration. |
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| Sample of a colour coded PSII structure, where the distance between the aligned photosystem II structures 1S5L.pdb (London) and 2AXT.pdb are mapped on the corresponding atoms of the more recent structure (2AXT). The 2S5L structure is shown in silver. To allow a better visualization the alpha carbons got mapped with the colour corresponding to the maximum displacement. The colour code is used for the following pictures. |
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