Testis-specific chromodomain protein Y 2
2fw2 C 62 C 63
A redox-regulated disulphide may form within Testis-specific chromodomain protein Y 2 between cysteines 343 and 344 (62 and 63 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2fw2
Structure name
catalytic domain of cdy
Structure deposition date
2006-01-31
Thiol separation (Å)
6
Half-sphere exposure sum ?
80
Minimum pKa ?
11
% buried
88
Peptide accession
Q9Y6F7
Residue number A
343
Residue number B
344
Peptide name
Testis-specific chromodomain protein Y 2
Ligandability
Cysteine 343 of Testis-specific chromodomain protein Y 2
Cysteine 344 of Testis-specific chromodomain protein Y 2
2fw2 C 147 C 233
A redox-regulated disulphide may form within Testis-specific chromodomain protein Y 2 between cysteines 428 and 514 (147 and 233 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
2fw2
Structure name
catalytic domain of cdy
Structure deposition date
2006-01-31
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
13
% buried
100
Peptide accession
Q9Y6F7
Residue number A
428
Residue number B
514
Peptide name
Testis-specific chromodomain protein Y 2
Ligandability
Cysteine 428 of Testis-specific chromodomain protein Y 2
Cysteine 514 of Testis-specific chromodomain protein Y 2
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