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o60294_02-2zwa_b (-)
Residue ID: 18
Variant: ASP > ASN
Detailed analysis
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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 does not introduce a proline.
Criterion: The substitution introduces a buried proline.
This substitution does not trigger clash alert. The local clash score for wild type is 96.27 and the local clash score for mutant is 96.15.
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 ASP is exposed hydrophilic with RSA 69.9% and the mutant residue ASN is exposed hydrophilic with RSA 46.4%.
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 ASP is exposed charged with RSA 69.9% and the mutant residue ASN is exposed uncharged with RSA 46.4%.
Criterion: The substitution replaces a buried uncharged residue with a charged residue.
This substitution does not alter the secondary structure 'T' (hydrogen bonded turn).
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 ASP is exposed negative-charged with RSA 69.9% and the mutant residue ASN is exposed uncharged with RSA 46.4%.
Criterion: The substitution switches the charge (+/-) of the buried residue.
This substitution does not trigger disallowed phi/psi alert. The phi/psi angles are in favored region for wild-type residue and in favored 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 ASP is exposed charged with RSA 69.9% and the mutant residue ASN is exposed uncharged with RSA 46.4%.
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.
The wild-type residue is not involved in any side-chain / side-chain H-bond(s) and/or side-chain / main-chain bond(s) H-bonds.
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.
Wild-type salt bridge is detected between OE1 atom of GLU 188 and NZ atom of LYS 24 (distance: 3.496 Å). However, salt bridge is also found in mutant structure between OE1 atom of GLU 188 and NZ atom of LYS 24 (distance: 3.496 Å). The wild-type residue is exposed (RSA 69.9%).
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 1.08 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 ASP is exposed (RSA 69.9%) and the mutant residue ASN is exposed (RSA 46.4%).
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).