In Depth Variant Analysis:  c.1778C>T (p.Thr593Met)
Terms with a '*' next to them are explained on the Help Page .
c.1778C>T
p.Thr593Met (Legacy AA No. 575)
Variant Type:  
Point
Domain:  
Serine Protease
Codon Change: 
C>T
Variant Effect: 
Missense
No. of Patients Reported: 
8
Phenotype: 
II
Allele Count *: 
10
Allele Number *: 
251488
Allele Frequency *: 
0.000040
Variant Comments & Reference:
Expression studies confirm that Thr593Met is a type II (CRM+) variant with a loss of functional activity most likely due to disruption of the catalytic domain. Thr593 in the catalytic domain is highly conserved. Molecular modeling predicts that the introduction of Met at position 593 results in the formation of a new hydrogen bond with Ser575, one of the residues that make up the serine protease catalytic triad in the FXI protein. Mitchell et al 2007Residue Information:
Name | Type | Cyclic | Size | Position | Hydrophobicity | Charge | |
---|---|---|---|---|---|---|---|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Substitution Analysis:
Structural Implications:
Thr593 is a buried residue  (surface accessibility value = 1 ).
Thr593 is in a region of secondary structure within the FXI domains.
The DSSP assignment for this residue is ... E.
Thr593 is in a region of secondary structure within the FXI domains.
The DSSP assignment for this residue is ... E.
Hint: Left click mouse | To rotate the structure
Hint: Rotate mousewheel | To zoom in/out the structure
Hint: Right click mouse | to use applet control options
|
Spacefill | |
Cartoon | |
Wireframe | |
Trace | |
Backbone | |
Spin | |
Background | |
Disulphides | |
Domains | |
Alternative Colouring | |
Labels |
Right Click on the molecule's screen for more options.
NOTE: If no Java applet appears or a Java error message is shown, please click the following LINK.