 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](rf5010fig2mag.jpg)
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Figure 2
Global improvement of the PfOMPDC structure upon refitting. (a) The percentage of residues in the most favored region of Ramachandran space (solid lines) is increased in all cases. The all-atom clashscore (dotted lines), as a percentile score among all structures in the PDB, is dramatically increased. (b) An apoenzyme region originally modeled in PDB entry 2za2 (white) as an extended loop, owing to a residue with the backbone carbonyl misaligned, is shown by the re-refined structure (gray) to form a typical α-helix with backbone atoms positioned within hydrogen-bonding distance (shown by the gray spring). (c) Comparison of the protein backbone near the active site shows potentially important differences (arrows) that change the shape of the binding pocket. Residues in PDB entry 2za2 (white) that would be within 5 Å of the substrate (orange, modeled from PDB entry 2za1) are compared with those of the re-refined apoenzyme structure (gray). |
![[Figure 2]](rf5010fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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