General Structure Information
| PDB ID | 2vom |
| HGNC Gene Label(s) | TPI1 |
| Structure Name | structural basis of human triosephosphate isomerase deficiency. mutation e104d and correlation to solvent perturbation. |
| Resolution | 1.85Å |
| Reference | AUTH C.RODRIGUEZ-ALMAZAN,R.ARREOLA-ALEMON,AUTH 2 D.RODRIGUEZ-LARREA,B.AGUIRRE-LOPEZ,AUTH 3 M.T.DE GOMEZ-PUYOU,R.PEREZ-MONTFORT,M.COSTAS,AUTH 4 A.GOMEZ-PUYOU,A.TORRES-LARIOSTITL STRUCTURAL BASIS OF HUMAN TRIOSEPHOSPHATETITL 2 ISOMERASE DEFICIENCY: MUTATION E104D IS RELATED TOTITL 3 ALTERATIONS OF A CONSERVED WATER NETWORK AT THETITL 4 DIMER INTERFACE.REF J.BIOL.CHEM. V. 283 23254 2008REFN ISSN 0021-9258PMID 18562316DOI 10.1074/JBC.M802145200 |
Variant Set Distributions
ExAC Variants
| Number Of Residues | 246 |
| Number Of SNVs | 52 |
| Number Of Permutations | 14297 |
| Optimal Distance Threshold | 15.0 |
| K Statistic | 0.262 |
| p-value | 0.154 |
ClinVar
| Number Of Residues | 246 |
| Number Of SNVs | 5 |
| Number Of Permutations | 742 |
| Optimal Distance Threshold | 8.0 |
| K Statistic | 0.0 |
| p-value | 0.819 |
Ripley’s K Analysis Plots
ExACClinVar
Variant Set Comparisons
ClinVar vs. ExAC
| Number Of ExAC SNVs | 52 |
| Number Of ClinVar SNVs | 5 |
| Optimal Distance Threshold | 8.0 |
| K Statistic | -0.044 |
| p-value | 1.0 |
Pathogenic Proximity Analysis
ClinVar PathProx Analysis
