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Figure 1.
Figure 1. Overall topology of the normal AGT dimer. (A) and
(B) The a-chain is colour-coded as follows: magenta, extended
N-terminal segment; red, large N-terminal domain; green, small
C-terminal domain. The b-chain is colour coded as follows: cyan,
extended N-terminal segment; yellow, large N-terminal domain;
blue, small C-terminal domain. B is rotated 180° in the
horizontal plane relative to A. Residues 41, 82, 170, 205, 209,
and 244 are indicated on the a-chain, residue 11 is indicated on
the b-chain. (C) Stereo pair of C^a chain, same orientation as
A. The pyridoxal phosphate cofactor is in shown in red and the
amino-oxyacetic acid inhibitor is shown in orange. The N and
C-terminal residues identified in the structure (4 and 390,
respectively) and every other 50 residues are numbered on the
a-chain (green).
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