A265C |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
A265V |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
A391T |
naturally occuring mutation, the mutation disrupts the hydrophobicity of the region |
Homo sapiens |
A434V |
naturally occuring mutation, the mutation causes steric clashes with the heme rendering the enzyme almost inactive |
Homo sapiens |
C169R |
naturally occuring mutation, the mutation alters the region's hydrophobicity, conserved residue C169 makes hydrophobic interactions with the loop between E-F helices and F-helix |
Homo sapiens |
D322G |
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure |
Homo sapiens |
D407N |
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure |
Homo sapiens |
E320K |
naturally occuring mutation, the mutation of E320, which is a highly conserved residue on a negatively charged Glu-Glu-Leu-Asp (EELD) motif, alters the charge on the motif |
Homo sapiens |
E431K |
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure |
Homo sapiens |
F404S |
naturally occuring mutation, the mutation prevents stable packing interactions resulting in salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
G178A |
naturally occuring mutation, the mutation causes reduced structural flexibility of the sharp fold between the E- and F-helices |
Homo sapiens |
G291C |
naturally occuring mutation, the mutation abolishes substrate binding causing salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
G291R |
naturally occuring mutation, the mutation abolishes substrate binding causing salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
G291S |
naturally occuring mutation, the mutation abolishes substrate binding causing salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
G292D |
naturally occuring mutation, the mutation abolishes substrate binding causing salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
G424S |
naturally occuring mutation, the mutation imparts rigidity to the loop between K'- and L-helix |
Homo sapiens |
G56R |
naturally occuring mutation, P57 and G56 form the hinge between the membrane interacting N-terminus and rest of the protein. The substitution of G56 with a polar and rigid Arg residue disrupts the hinge affecting the interactions of CYP21A2 with the membrane |
Homo sapiens |
G90V |
naturally occuring mutation, mutation of G90 to valine affects the ability of R91 to hydrogen bond with heme, causing salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
H119R |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
H365Y |
naturally occuring mutation, the mutations causes the salt-wasting disease |
Homo sapiens |
H62L |
naturally occuring mutation, the mutation may disrupt hydrogen bonding to reduce, but not eliminate, enzyme activity |
Homo sapiens |
I172N |
naturally occuring mutation, the mutation causes a loss of the hydrophobic pocket, I172 forms a hydrophobic pocket with M186 and M187 residues of F-helix |
Homo sapiens |
I194N |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
I230T |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
I77T |
naturally occuring mutation, the mutation disrupts the hydrophobic environment |
Homo sapiens |
K121Q |
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase |
Homo sapiens |
L107R |
naturally occuring mutation, the mutation abolishes heme binding and causes salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
L142P |
naturally occuring mutation, the mutation of the D-helix causes helical disruption and destabilization of secondary structures |
Homo sapiens |
L166P |
naturally occuring mutation, the mutation of the E-helix causes helical disruption and destabilization of secondary structures |
Homo sapiens |
L167P |
naturally occuring mutation, the mutation of the E-helix causes helical disruption and destabilization of secondary structures |
Homo sapiens |
L261P |
naturally occuring mutation, the mutation of the H-helix causes helical disruption and destabilization of secondary structures |
Homo sapiens |
L300F |
naturally occuring mutation, the mutation causes localized destabilization of secondary structure |
Homo sapiens |
L307M |
naturally occuring mutation, the mutation disrupts the optimal packing of side chains but does not alter the hydrophobic environment |
Homo sapiens |
L307V |
naturally occuring mutation, the mutation disrupts the optimal packing of side chains but does not alter the hydrophobic environment |
Homo sapiens |
L308F |
naturally occuring mutation, the mutation causes localized destabilization of secondary structure |
Homo sapiens |
L353R |
naturally occuring mutation, the mutation abolishes heme binding and causes salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
L363W |
naturally occuring mutation, the mutation causes steric clashes with the heme rendering the enzyme almost inactive |
Homo sapiens |
L446P |
naturally occuring mutation, the mutation of the L-helix causes helical disruption and destabilization of secondary structures |
Homo sapiens |
N387K |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
P30E |
naturally occuring mutation causing disruption of the interaction between the carbon of P30 in the N-terminal loop and the side chain of Y376 within the beta5-beta6 hairpin loop resuting in the salt-wasting disease |
Homo sapiens |
P432L |
naturally occuring mutation, the mutation makes the structure more flexible and prevents cysteine from being presented to heme |
Homo sapiens |
P453S |
naturally occuring mutation, the mutation disrupts the hydrophobicity of the region |
Homo sapiens |
P459H |
naturally occuring mutation, the mutation disrupts the hydrophobicity of the region |
Homo sapiens |
P463L |
naturally occuring mutation, the mutation interferes with the conformation of the beta8-beta9 loop with the subsequent closure of substrate entrance channel |
Homo sapiens |
Q481P |
naturally occuring mutation, the mutation destabilizes the structure rendering the protein inactive |
Homo sapiens |
R124H |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
R132C |
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase |
Homo sapiens |
R149C |
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure |
Homo sapiens |
R233G |
naturally occuring mutation, the mutation may prevent R233 from binding to the 3-keto oxygen of the proximal 17OHP in the proper orientation, it does not influence protein activity significantly, resulting in minimal phenotype |
Homo sapiens |
R233K |
naturally occuring mutation, the mutation may prevent R233 from binding to the 3-keto oxygen of the proximal 17OHP in the proper orientation, it does not influence protein activity significantly, resulting in minimal phenotype |
Homo sapiens |
R339H |
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase |
Homo sapiens |
R341P |
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase |
Homo sapiens |
R341W |
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase |
Homo sapiens |
R356P |
naturally occuring mutation, the mutation disrupts the interaction of R356 with Q389 rendering the enzyme inactive and causing salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
R369Q |
naturally occuring mutation, the mutation impairs the interaction with the P450 oxidoreductase |
Homo sapiens |
R408C/L |
naturally occuring mutation, the mutation destabilizes structural elements because of the extensive loss of hydrogen bonds |
Homo sapiens |
R408H |
naturally occuring mutation, the mutation prevents normal hydrogen bonding with E351 and R354 |
Homo sapiens |
R426C |
naturally occuring mutation, the mutation disrupts the interaction of residues R91 and R426 rendering the protein nonfunctional and causing salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
R435C |
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure |
Homo sapiens |
R479L |
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure |
Homo sapiens |
R483P |
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure |
Homo sapiens |
R483Q |
naturally occuring mutation, the mutation prevents salt bridge formation resulting in a localized, as opposed to global, destabilization of tertiary structure |
Homo sapiens |
S301Y |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
T168N |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
T295X |
naturally occuring mutation, the mutation abolishes substrate binding and causes salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
T450P |
naturally occuring mutation, the mutation reduces flexibility of beta8-sheet, which helps stabilize the very long C-terminal loop |
Homo sapiens |
V139E |
naturally occuring mutation, mutation to glutamate disrupts the interaction with residues V440 and L436 on the L-helix causing instability of the enzyme, charge repulsions between the side chain of mutated V139E and E437 of the E-helix render the protein unstable and inactive causing salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
V249A |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
V281G |
naturally occuring mutation, the mutation causes a loss of the hydrophobic pocket |
Homo sapiens |
V304M |
naturally occuring mutation, the mutation causes side-chain steric clashes with the neighboring residues |
Homo sapiens |
W302R |
naturally occuring mutation, the mutation prevents stable packing interactions resulting in salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
W302S |
naturally occuring mutation, the mutation prevents stable packing interactions resulting in salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
Y47C |
naturally occuring mutation, the mutation disables hydrogen bonding with H38, the interaction is compensated by a weak His-Cys interaction |
Homo sapiens |
Y47L |
naturally occuring mutation, the mutation disrupts hydrogen bonds and causes salt-wasting congenital adrenal hyperplasia |
Homo sapiens |
Y59N |
naturally occuring mutation, the mutation disrupts the hydrophobicity of the region resulting in loss of function |
Homo sapiens |