Please note that you can explore the 3D structure of the molecule and your missense variant by using the mouse to rotate and zoom. You can also use the options in the "Display Control" next to the molecular viewer.
o15389_02-5lf5_a (-)
Residue ID: 333
Variant: SER > PRO
Disallowed phi/psi
Detailed analysis
Click on each feature for further information
The wild-type residue is not CYS so it cannot form a disulphide bond.
Criterion: The substitution breaks a disulphide bond that was in the wild-type. The maximum S-S length for the bond is 3.3 Å.
This substitution introduces a proline but it's on the surface.
Criterion: The substitution introduces a buried proline.
This substitution does not trigger clash alert. The local clash score for wild type is 133.72 and the local clash score for mutant is 137.14.
Criterion: The mutant structure has a MolProbity clash score ≥ 30 and the increase in clash score is > 18 compared to the wild type.
This substitution does not replace a buried hydrophobic residue with a hydrophilic residue. The wild-type residue SER is exposed neutral with RSA 22.3% and the mutant residue PRO is exposed neutral with RSA 11.0%.
Criterion: The substitution replaces a buried hydrophobic residue with a hydrophilic residue.
This substitution does not trigger buried uncharged residue alert. The wild-type residue SER is exposed uncharged with RSA 22.3% and the mutant residue PRO is exposed uncharged with RSA 11.0%.
Criterion: The substitution replaces a buried uncharged residue with a charged residue.
This substitution does not alter the secondary structure ' ' (no secondary structure).
Criterion: A substitution results in a change in the DSSP secondary structure assignment at the variant position.
This substitution does not trigger buried charge switch alert. The wild-type residue SER is exposed uncharged with RSA 22.3% and the mutant residue PRO is exposed uncharged with RSA 11.0%.
Criterion: The substitution switches the charge (+/-) of the buried residue.
This substitution triggers disallowed phi/psi alert. The phi/psi angles are in favored region for wild-type residue but outlier region for mutant residue.
Criterion: The mutant residue is in outlier region while the wild-type residue is in the favoured or allowed region.
This substitution does not replace a buried charged residue with an uncharged residue. The wild-type residue SER is exposed uncharged with RSA 22.3% and the mutant residue PRO is exposed uncharged with RSA 11.0%.
Criterion: The substitution replaces a buried charged residue with an uncharged residue.
This substitution does not replace a buried GLY residue.
Criterion: The substitution replaces a buried glycine.
This substitution does not result in a complete disruption of all side-chain / side-chain H-bond(s) and/or side-chain / main-chain bond(s) bonds, and the wild-type residue is not buried (RSA 22.3%).
Criterion: The substitution breaks all side-chain / side-chain H-bond(s) and/or side-chain / main-chain H-bond(s) formed by the wild type which was buried. The maximum H-bond N-O length is 3.9 Å.
The wild-type residue does not form any salt bridge.
Criterion: The substitution breaks a salt bridge formed by wild-type which was buried. The maximum N-O bond length is 5.0 Å.
The substitution leads to the expansion of cavity volume by 0.432 Å^3.
Criterion: The substitution leads to an expansion or contraction of the cavity volume of ≥ 70 Å^3. Cavity also refers to a pocket on the surface.
The wild-type residue SER is exposed (RSA 22.3%) and the mutant residue PRO is exposed (RSA 11.0%).
Criterion: The substitution results in a change between buried and exposed state of the target variant residue. (RSA < 9% for buried and the difference between RSA has to be at least 5%.)
Wild-type residue is not a cis proline.
Criterion: A cis proline in the wild type is replaced in the mutant.
The wild-type residue is not GLY.
Criterion: The wild-type residue is glycine and is located in a bend curvature (reported 'S' in DSSP).