 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](ow5019fig1mag.jpg)
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Figure 1
Structure of the omalizumab Fab (FabXol). (a) The FabXol1 structure contains one Fab molecule (pink and blue) in the asymmetric unit. The heavy-chain CDRs of this Fab contact the VL and Cκ domains (the latter hidden in this view) of one symmetry-related molecule (green and yellow) and the Cκ domain of another (orange and gray). (b) Interface between heavy-chain CDR residues (blue) and VL and Cκ domain framework residues from a symmetry-related molecule (green) in the FabXol1 structure. Hydrogen bonds are depicted by black lines. (c) Interface between an edge β-strand from the Cγ1 domain (blue) and the Cκ domain from a symmetry-related molecule (orange) in the FabXol1 structure. Hydrogen bonds are depicted by black lines. (d) Interface between heavy-chain CDR residues (gray) and VL and Cκ domain framework residues from a symmetry-related molecule (yellow) for FabXol2B, which includes a hydrogen bond between His101 (CDRH3) and Gln81 (VL domain). Hydrogen bonds are depicted by black lines. |
![[Figure 1]](ow5019fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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