 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 7]](wd5214fig7mag.jpg)
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Figure 7
The common intermolecular interfaces between the TBNAT (PDB entry 4bgf ) and MMNAT (PDB entry 2vfb ) apoprotein crystal structures as calculated using the PISA web server (https://www.ebi.ac.uk/msd-srv/prot_int/ ). The symmetry operator indicates the index of crystallographic symmetry-related molecules in the MMNAT structure participating in protein–protein interface contacts. The number in parentheses shows the symmetry operator index with the translation vector in fractional units. Interactions participating in the interface region are marked H for hydrogen bond and/or S for salt bridge. In the software tool PISA, interfacing atoms (atoms within interfacing residues) are those atoms which are exposed to another molecule and not to the solvent and they may be involved in bonding across the interface. Not all of the atoms in an interfacing residue will be involved in interface formation or contact. Some may be exposed to the solvent and some may be inaccessible. The PISA bonding criteria are that a hydrogen bond is present if the distance between the donor and acceptor atoms is less than 3.89 Å and a salt bridge if the interacting atoms are within 4 Å. The listed residues are these that participate in the interface region in the MMNAT sequence. Residues that are different from those of the TBNAT sequence are highlighted in blue. |
![[Figure 7]](wd5214fig7.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
