PHD finger protein 7
Intramolecular
Cysteine 273 and cysteine 300
Cysteine 273 and cysteine 276
Cysteine 273 and cysteine 297
Cysteine 248 and cysteine 253
Cysteine 248 and cysteine 285
Cysteine 253 and cysteine 285
Cysteine 276 and cysteine 300
Cysteine 297 and cysteine 300
Cysteine 276 and cysteine 297
1weq A 49 A 76
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 273 and 300 (49 and 76 respectively in this structure).
Details
Redox score ?
89
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
5
% buried
2
Peptide accession
Q9DAG9
Residue number A
273
Residue number B
300
Peptide name
PHD finger protein 7
Ligandability
Cysteine 273 of PHD finger protein 7
Cysteine 300 of PHD finger protein 7
1weq A 49 A 52
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 273 and 276 (49 and 52 respectively in this structure).
Details
Redox score ?
88
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
2
Peptide accession
Q9DAG9
Residue number A
273
Residue number B
276
Peptide name
PHD finger protein 7
Ligandability
Cysteine 273 of PHD finger protein 7
Cysteine 276 of PHD finger protein 7
1weq A 49 A 73
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 273 and 297 (49 and 73 respectively in this structure).
Details
Redox score ?
87
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
4
Peptide accession
Q9DAG9
Residue number A
273
Residue number B
297
Peptide name
PHD finger protein 7
Ligandability
Cysteine 273 of PHD finger protein 7
Cysteine 297 of PHD finger protein 7
1weq A 24 A 29
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 248 and 253 (24 and 29 respectively in this structure).
Details
Redox score ?
85
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
12
Peptide accession
Q9DAG9
Residue number A
248
Residue number B
253
Peptide name
PHD finger protein 7
Ligandability
Cysteine 248 of PHD finger protein 7
Cysteine 253 of PHD finger protein 7
1weq A 24 A 61
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 248 and 285 (24 and 61 respectively in this structure).
Details
Redox score ?
84
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
64
Minimum pKa ?
7
% buried
22
Peptide accession
Q9DAG9
Residue number A
248
Residue number B
285
Peptide name
PHD finger protein 7
Ligandability
Cysteine 248 of PHD finger protein 7
Cysteine 285 of PHD finger protein 7
1weq A 29 A 61
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 253 and 285 (29 and 61 respectively in this structure).
Details
Redox score ?
82
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
56
Minimum pKa ?
9
% buried
14
Peptide accession
Q9DAG9
Residue number A
253
Residue number B
285
Peptide name
PHD finger protein 7
Ligandability
Cysteine 253 of PHD finger protein 7
Cysteine 285 of PHD finger protein 7
1weq A 52 A 76
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 276 and 300 (52 and 76 respectively in this structure).
Details
Redox score ?
82
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
37
Minimum pKa ?
8
% buried
0
Peptide accession
Q9DAG9
Residue number A
276
Residue number B
300
Peptide name
PHD finger protein 7
Ligandability
Cysteine 276 of PHD finger protein 7
Cysteine 300 of PHD finger protein 7
1weq A 73 A 76
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 297 and 300 (73 and 76 respectively in this structure).
Details
Redox score ?
82
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
3
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
2
Peptide accession
Q9DAG9
Residue number A
297
Residue number B
300
Peptide name
PHD finger protein 7
Ligandability
Cysteine 297 of PHD finger protein 7
Cysteine 300 of PHD finger protein 7
1weq A 52 A 73
A redox-regulated disulphide may form within PHD finger protein 7 between cysteines 276 and 297 (52 and 73 respectively in this structure).
Details
Redox score ?
79
PDB code
1weq
Structure name
solution structure of phd domain in phd finger protein 7
Structure deposition date
2004-05-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
2
Peptide accession
Q9DAG9
Residue number A
276
Residue number B
297
Peptide name
PHD finger protein 7
Ligandability
Cysteine 276 of PHD finger protein 7
Cysteine 297 of PHD finger protein 7
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