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Figure 1.
Figure 1. Structures of glucosamine 6-phosphate deaminase from
P. furiosus. (A) A polypeptide chain consisted of two similar
five-stranded subdomains and C-terminal tail. N-terminal
subdomain (red and yellow) and C-terminal subdomain (blue and
magenta) were linked by short loop (gray) were followed by long
C-terminal coil region (gray). (B) Twofold symmetrical
interaction of two polypeptide chains (green and blue). A helix
(yellow) from one chain interacts a cleft between N- and
C-terminal subdomains of another chain (B_Nt and B_Ct) forming
an active site (red circle). (C) A substrate, glucosamine
6-phosphate (yellow) from crystal structure of the isomerase of
E. coli GlmS was superimposed on the active site of GlmD
consisted of both monomers (green and blue). (D) C-terminal tail
covers the substrate-binding site between two monomers (blue and
green). Glucosamine 6-phosphate is placed to the binding pocket.
Residue from other than a molecule containing sugar-binding site
are indicated by asterisk. Residues D320, R324, and W325 from
C-terminal region interact to K230, R226, and W249 from another
monomer.
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