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5.3.3.17
dimer
2 * 32218, histidine-tagged enzyme
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702206
5.3.3.17
dimer
deduced from crystal structure. The crystal structure clarifies that the enzyme is a dimer in an up/up configuration with the two active sites facing each other. The dimer in the open form, generates by crystal symmetry (sulfate complex), interacts mainly through the alpha1-helices and the beta16-strands in the N-terminal domains. The C-terminal domains are not in direct contact but are relatively close
706479
5.3.3.17
homodimer
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749064
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