Table 2. Direct interactions between protein residues at the MauG–MADH interface.
Only those interactions that are conserved between the independent copies of MauG and MADH at distances of less than 4 Å and for which there is strong electron density are listed, except where noted in the text. Specific values are for the B chain of MauG. The designation α′ indicates that the residue comes from the other α-subunit.
| Protein–protein interactions | Distance (Å) | |||||
|---|---|---|---|---|---|---|
| MADH residue | MauG residue | Interaction type | MauG–preMADH | MauG–TTQOQ MADH (C2) | MauG–TTQOQ MADH (P21) | MauG–TTQOX MADH |
| αAsp180 | Arg338 | Salt bridge | 3.0 | 3.0 | 3.0 | 3.1 |
| αPro158 | Met333 | Hydrogen bond | 2.9 | 2.8 | 2.9 | 2.9 |
| αSer157 | Gly331 | Hydrogen bond | 2.6 | 2.4 | 2.5 | 2.5 |
| αArg197 | Phe191 | π-Stacking | 3.7 | 3.7 | 3.7 | 3.3 |
| α′Gly29 | Arg208 | Hydrogen bond | 3.1 | 3.0 | 2.7 | 2.9 |
| α′Asp31 | Lys209 | Hydrogen bond | 2.9 | 3.2 | 3.1 | 3.1 |
| α′Asp31 | Gln210 | Hydrogen bond | 3.0 | 3.0 | 3.0 | 3.1 |
| βGlu101 | Arg338 | Salt bridge | 2.7 | 2.8 | 2.8 | 2.6 |
| βGlu101 | Trp199 | Hydrogen bond | 3.4 | 3.5 | 3.2 | 3.1 |
| βIle126 | Gly211 | Hydrogen bond | 2.9 | 2.8 | 2.8 | 2.8 |
| βThr54 | Arg202 | Hydrogen bond | 2.8 | 4.1 | 4.8 | 2.7 |
| βSer56 | Thr198 | Hydrogen bond | 3.0 | 3.7 | 3.9 | 3.3 |
| βThr44 | Gln210 | Hydrogen bond | 3.4 | 3.2 | 3.2 | 3.3 |