 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](dw5120fig3mag.jpg)
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Figure 3
Close-up view of the nonreducing end of heparin chain a with Δ4UAp2S. The stereo panels show a close-up view of the centre of the antiparallel (APLP1 E2)2 assembly. Selected amino-acid side chains involved in heparin binding are shown as stick models and are coloured according to the individual protein chains in magenta (chain a) or in cyan (chain b). C atoms of individual heparin chains are coloured likewise. Specific interactions between amino-acid side chains and sugar residues are highlighted with orange dashes. Amino-acid side chains and sugar residues are numbered. (a) The Fo − Fc kicked heparin OMIT electron-density map is contoured at 3.5σ (green mesh). (b) Substitution of Δ4UAp2S by IdoAp2S at the nonreducing end of heparin chain a. Colours are as in (a). The final structure with Δ4UAp2S at the nonreducing end [as shown in (a)] is shown for comparison as a grey-coloured ball-and-stick model. The Fo − Fc kicked heparin OMIT electron-density map is contoured at −4.0σ (red mesh). |
![[Figure 3]](dw5120fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
