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![[Figure 9]](ba5257fig9mag.jpg)
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Figure 9
Glycosidic bonds, distortion in the −1 subsite and mutarotation at the reducing end. The figure shows the active site of an α-mannanase enzyme reported by Thompson et al. (2015  , 2016), which was crystallized in complex with α1–6-mannopentaose. Sugars have been numbered according to standard practice, from 500A (and its alternate configuration, 500B) at the reducing end to 504 (not shown) at the nonreducing end. LINK records can be defined as shown in the inset (only the part relevant to residue identification is shown; see the PDB format specification for the full syntax) and have to be replicated to link both configurations of residue 500, which in turn have their respective occupancies reduced to 0.5. The sugar in the −1 subsite (nomenclature defined in Davies et al., 1997) is distorted by the catalytic residues (not shown) to a B2,5 conformation, which is well supported by clear electron density and described by QM/MM metadynamics simulations as part of the catalytic itinerary (Thompson et al., 2015, 2016). This figure was generated with CCP4mg (McNicholas et al., 2011). |
![[Figure 9]](ba5257fig9.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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