E(Ain) |
Forms stable H-bonds with TRPS. Waters are stable in the binding site. |
Fewer waters around the PO, which affects the proton delivery. |
|
H-bonds between PN and Ser377 are missing. Lys87 side chain rotates. |
H-bonds between PN and Ser377 are missing. Lys87 side chain rotates. |
E(A-A) |
Gln114 side chain tends to form H-bonds with PO. |
PG, PN and CO form stable interactions with TRPS. |
H-bonds between CO and Thr110 are missing. |
H-bonds between PN and Ser377 are missing. |
Thr190 and Ser235 loop moves. Salt-bridge (Arg141-Asp305) can- not be retained. |
E(Q)indoline
|
Gln114 side chain occasionally forms H-bonds with PO. |
PG, PN and CO form stable interactions with TRPS. |
H-bonds between CO and Thr110 remain. Substrate is stable in the binding site. |
H-bonds between PN and Ser377 are missing. |
|
E(Q)2AP
|
Gln114 side chain occasionally forms H-bonds with PO. |
PG, PN and CO form stable interactions with TRPS. |
H-bonds between CO and Thr110 are missing. Substrate is stable in the binding site. |
H-bonds between PN and Ser377 are missing. |
|