TABLE 2.
AgamOBP48 residues lining the central cleft and the two channels
EN12 is predicted to bind into the central cleft of the AgamOBP48 monomer. The combined PEG-binding site is part of Channel 1 and is found only in the dimer. A single copy of the NC-term binding pocket is present in the monomer. In the dimer, the NC-term pocket is duplicated and forms part of Channel 2. The residues that interact with the PEG molecule (P) in the crystal structure, and those that interact with the compound EN12 (L) in the modeled complexes are represented in bold.
| Central cleft, chain A | Channel 1 (PEG site),a chain A/B | Channel 2 (NC-term pockets), chain A/B |
|---|---|---|
| Lys-21 (L) | Gly-49 | Pro-15 (L) |
| Pro-22 (L) | Ile-50 | Cys-18 (L) |
| Met-23 (L) | Pro-51 | Cys-19 (L) |
| Leu-24 (L) | Pro-89 | Leu-45 (L)a |
| Val-25 (L) | Glu-90 | Ile-50 |
| Gly-27 (L) | Ser-93 | Pro-51 |
| Met-30 (L) | Leu-94 | Glu-90 |
| Met-31 (L) | Leu-105 (P/L) | Ser-93 |
| Leu-137 (L) | Lys-109 (P) | Leu-94 |
| Met-140 (L) | Glu-112 | Lys-109 |
| Gly-141 (L) | Ile-113 | Glu-112 |
| Met-144 (L) | Pro-131 | Met-142 |
| Gly-134 (L) | Phe-145 (L) | |
| Thr-135 (P/L) | Ala-146 (L) | |
| Arg-138 (P/L) | Gln-147 | |
| Cys-139 (P/L) | Cys-148 (L) | |
| Met-142 (P/L) | Pro-149 | |
| Met-143 (L) | Ala-150 (L) | |
| Ala-146 (P/L) | Ser-151 | |
| Gln-147 (L) | Phe-153 (L) | |
| Pro-149 | Leu-162 (L) | |
| Ala-150 | Arg-163 (L) | |
| Ser-151 | Gly-166 | |
| Ser-167 (L) |
a In the dimer only.