Table 5. Comparison of the TcruCA dimeric interface.
All data were calculated using PDBePISA (Krissinel Henrick, 2007 ▸).
| Dimeric -CA | PDB code | Interface area† (2) | No. of interfacing residues‡ | G solv (kcalmol1) | G solv P-value | No. of hydrogen bonds |
|---|---|---|---|---|---|---|
| TcruCA | 4xz5 | 898 | 63 (31, 32) | 9.7 | 0.123 | 18 |
| hCA VI | 3fe4 | 869 | 54 (28, 26) | 9.8 | 0.552 | 11 |
| hCA IX | 3iai | 802 | 54 (27, 27) | 9.0 | 0.227 | 2 |
| hCA XII | 1jcz | 1130 | 72 (35, 37) | +1.1 | 0.783 | 17 |
| SspCA | 4g7a | 1162 | 67 (35, 32) | 12.8 | 0.050 | 11 |
| Cr-CA1 | 3b1b | 1493 | 84 (42, 42) | 17.7 | 0.068 | 21 |
| AoCA | 3q31 | 1812 | 93 (46, 47) | 18.4 | 0.189 | 23 |
†
Calculated as the difference in the total accessible surface areas of isolated and interfacing structures divided by two.
‡
Values in parentheses correspond to the numbers of residues from each monomer.
§
Solvation free-energy gain upon formation of the interface. G solv 0 corresponds to positive protein affinity by hydrophobic interfaces (excludes contributions from salt bridges and hydrogen bonds).
¶
Measure of the likelihood of the interface forming as a result of crystal packing. Note that G solv P-values of >0.5 indicate that the interface is likely to be an artifact of crystal packing and not biological in nature.