 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](hv5046fig1mag.jpg)
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Figure 1
Structural overview. (a) Ribbon diagram of the mAng–SO4 structure. Helices are coloured yellow and β-strands pink. Disulfide bonds (blue) and a sulfate ion (red) bound to the active site are shown in ball-and-stick representation. Elements of secondary structure are labelled, as are the N- and C-terminal extremities of the Cα chain (residues 3 and 119, respectively). The disulfide bonds are formed between residues 39 and 91 (top), 26 and 80 (middle) and 57 and 106 (bottom). (b) Structure-based alignment of hAng, mAng, bAng and RNase A sequences. Elements of secondary structure are shaded according to the colour scheme in (a) and labelled below. In the RNase A sequence, residues shown crystallographically to form the B1 and B2 subsites are coloured green and blue, respectively, while those that form the P1 subsite are ringed in red. hAng residue numbers are given above the sequences and RNase A residue numbers below. `<Q' signifies a pyroglutamate residue. |
![[Figure 1]](hv5046fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
