Table 1 Functional contribution of sectors defined for the ptRNase superfamily.
From: Conserved amino acid networks modulate discrete functional properties in an enzyme superfamily
IC | Residue mapping on 3D structure | Residue | Function | Reference |
|---|---|---|---|---|
1 |
| C26 | Stabilizing the conformation (S-S bond with C84) | |
C40 | Stabilizing the conformation (S-S bond with C95) | |||
F46 | Chain folding initiation site (CFIS) residue | |||
C58 | Stabilizing the conformation (S-S bond with C110) | |||
S75 | H-bonding with I106, Hydrophobic core | |||
C84 | Stabilizing the conformation (S-S bond with C84) | |||
C95 | Stabilizing the conformation (S-S bond with C40) | |||
Y97 | CFIS residue (fixes K41 through H-bonding) | |||
C110 | Stabilizing the conformation (S-S bond with C58) | |||
2 |
| K7 | P2 substrate binding site for endonuclease specificity | |
R10 | P2 substrate binding site for endonuclease specificity | |||
D14 | H-bonding with Y25 | |||
Y25 | Hydrophobic core, H-bonding with D14 | |||
M29 | Hydrophobic core | |||
R33 | H-bonding with R10 and M13 | |||
N34 | Part of N-glycosylation sequence (N34-L35-T36) | |||
T36 | Part of N-glycosylation sequence(N34-L35-T36) | |||
V47 | Hydrophobic core | |||
L51 | Hydrophobic core | |||
I106 | Hydrophobic core, expedites folding | |||
F120 | Hydrophobic core, fixes the side-chain of H119 | |||
3 |
| F8 | Juxtaposing His12 by π-interaction with His12 | |
Q11 | P1 substrate binding site | |||
H12 | Catalytic triad residue (General base for catalysis) | |||
M30 | Hydrophobic core | |||
K41 | Catalytic triad residue (H-bond with transition state) | |||
N44 | H-bonding with H12 and K41 | |||
T45 | Pyrimidine specificity of the B1 site | |||
N71 | B2 substrate binding site | |||
A109 | CFIS residue | |||
P117 | Trans-isomerization for folding | |||
V118 | CFIS residue | |||
H119 | Catalytic triad residue (General acid for catalysis) | |||
D121 | P1 substrate binding site |