Table 2.
Important residues found interacting with antipain in the structure of OPB [38]. The catalytic triad (
), residues involved in the S1 (
,
), S2 (
,
) and S3 (
) binding sites are highlighted and correspond to Figure 5. These residues are all conserved in OPB2.
| LmOPB Residue | AIP residue | Interaction | Importance |
|---|---|---|---|
|
| |||
|
Ser-577-OG |
P1-C | Covalent | Catalytic triad/S1 binding site |
|
Asp-662 |
n/a | n/a | Catalytic triad |
|
His-697 |
n/a | n/a | Catalytic triad |
|
Tyr-496-OH |
P1-O | Hydrogen-bond | Oxyanion/S1 binding site |
|
Ala-578-N |
P1-O | Hydrogen-bond | Oxyanion/S1 binding site |
|
Glu-621-OE1 |
P1-NE/NH2 | Hydrogen-bond | S1 binding site |
|
Arg-664-O |
P1-NH1 | Hydrogen-bond | S1 binding site |
|
Tyr-499-OH |
P1-N | Hydrogen-bond | S1 binding site |
|
Phe-603 |
P1 | pi-cation | S1 binding site |
|
Val-665 |
P1 | Hydrophobic | S1 binding site |
|
Arg-664-NH1 |
P2-O | Hydrogen-bond | S2-binding site |
|
Tyr-499 |
P2 | Hydrophobic | S2 binding site (predicted) |
|
Leu-617 |
P3 | Hydrophobic | S3-binding site |