Syncytin-1
Intramolecular
Cysteine 397 and cysteine 404
Cysteine 397 and cysteine 405
Cysteine 404 and cysteine 405
5ha6 A 397 A 404
A redox-regulated disulphide may form within Syncytin-1 between cysteines 397 and 404.
Details
Redox score ?
86
PDB code
5ha6
Structure name
crystal structure of human syncytin-1 fusion subunit
Structure deposition date
2015-12-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
36
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q9UQF0
Residue number A
397
Residue number B
404
Peptide name
Syncytin-1
Ligandability
Cysteine 397 of Syncytin-1
Cysteine 404 of Syncytin-1
6rx1 A 397 A 405
A redox-regulated disulphide may form within Syncytin-1 between cysteines 397 and 405. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
6rx1
Structure name
crystal structure of human syncytin 1 in post-fusion conformation
Structure deposition date
2019-06-07
Thiol separation (Å)
7
Half-sphere exposure sum ?
33
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UQF0
Residue number A
397
Residue number B
405
Peptide name
Syncytin-1
Ligandability
Cysteine 397 of Syncytin-1
Cysteine 405 of Syncytin-1
6rx1 A 404 A 405
A redox-regulated disulphide may form within Syncytin-1 between cysteines 404 and 405. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
6rx1
Structure name
crystal structure of human syncytin 1 in post-fusion conformation
Structure deposition date
2019-06-07
Thiol separation (Å)
8
Half-sphere exposure sum ?
28
Minimum pKa ?
9
% buried
nan
Peptide accession
Q9UQF0
Residue number A
404
Residue number B
405
Peptide name
Syncytin-1
Ligandability
Cysteine 404 of Syncytin-1
Cysteine 405 of Syncytin-1
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