 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](hv5268fig2mag.jpg)
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Figure 2
Comparison of liganded FABP4 structures. All values were calculated per amino-acid residue using the apoprotein structure as a reference. Each row corresponds to FABP4 protein with ligands L1 to L6, as indicated by the numbers on the left (from 1 to 6, respectively). Parameters calculated are the root-mean-square deviations of backbone atoms (`RMSD bb') and of backbone plus side-chain atoms (`RMSD bb+sch'), molecular surface area (`MSA'), curvature (`CUR') and accessible surface area (`ASA') of each protein without ligand. All parameter values are indicated by shading from white to black corresponding to the minimum and maximum values observed for each protein. In addition, curvature values are depicted as upward or downward triangles indicating positive or negative values, respectively. The protein sequence (bottom) is scaled to the protein topology diagram (top). Most changes are associated with mobile loops and residues with solvent-exposed side chains, indicative of minimal conformational changes upon ligand binding. |
![[Figure 2]](hv5268fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
