PHD finger protein 24
Intramolecular
Cysteine 185 and cysteine 188
Cysteine 133 and cysteine 158
Cysteine 133 and cysteine 136
Cysteine 150 and cysteine 188
Cysteine 150 and cysteine 185
Cysteine 136 and cysteine 158
Cysteine 147 and cysteine 150
Cysteine 147 and cysteine 188
Cysteine 147 and cysteine 185
5xht A 55 A 58
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 185 and 188 (55 and 58 respectively in this structure).
Details
Redox score ?
87
PDB code
5xht
Structure name
the phd finger of human kiaa1045 protein
Structure deposition date
2017-04-24
Thiol separation (Å)
3
Half-sphere exposure sum ?
43
Minimum pKa ?
9
% buried
9
Peptide accession
Q9UPV7
Residue number A
185
Residue number B
188
Peptide name
PHD finger protein 24
Ligandability
Cysteine 185 of PHD finger protein 24
Cysteine 188 of PHD finger protein 24
5xht A 3 A 28
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 133 and 158 (3 and 28 respectively in this structure).
Details
Redox score ?
84
PDB code
5xht
Structure name
the phd finger of human kiaa1045 protein
Structure deposition date
2017-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
7
% buried
4
Peptide accession
Q9UPV7
Residue number A
133
Residue number B
158
Peptide name
PHD finger protein 24
Ligandability
Cysteine 133 of PHD finger protein 24
Cysteine 158 of PHD finger protein 24
5xht A 3 A 6
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 133 and 136 (3 and 6 respectively in this structure).
Details
Redox score ?
84
PDB code
5xht
Structure name
the phd finger of human kiaa1045 protein
Structure deposition date
2017-04-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
7
% buried
4
Peptide accession
Q9UPV7
Residue number A
133
Residue number B
136
Peptide name
PHD finger protein 24
Ligandability
Cysteine 133 of PHD finger protein 24
Cysteine 136 of PHD finger protein 24
1wil A 35 A 73
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 150 and 188 (35 and 73 respectively in this structure).
Details
Redox score ?
83
PDB code
1wil
Structure name
solution structure of the ring finger domain of the human kiaa1045 protein
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
8
% buried
1
Peptide accession
Q9UPV7
Residue number A
150
Residue number B
188
Peptide name
PHD finger protein 24
Ligandability
Cysteine 150 of PHD finger protein 24
Cysteine 188 of PHD finger protein 24
1wil A 35 A 70
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 150 and 185 (35 and 70 respectively in this structure).
Details
Redox score ?
82
PDB code
1wil
Structure name
solution structure of the ring finger domain of the human kiaa1045 protein
Structure deposition date
2004-05-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
52
Minimum pKa ?
9
% buried
5
Peptide accession
Q9UPV7
Residue number A
150
Residue number B
185
Peptide name
PHD finger protein 24
Ligandability
Cysteine 150 of PHD finger protein 24
Cysteine 185 of PHD finger protein 24
1wil A 21 A 43
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 136 and 158 (21 and 43 respectively in this structure).
Details
Redox score ?
81
PDB code
1wil
Structure name
solution structure of the ring finger domain of the human kiaa1045 protein
Structure deposition date
2004-05-28
Thiol separation (Å)
3
Half-sphere exposure sum ?
39
Minimum pKa ?
10
% buried
0
Peptide accession
Q9UPV7
Residue number A
136
Residue number B
158
Peptide name
PHD finger protein 24
Ligandability
Cysteine 136 of PHD finger protein 24
Cysteine 158 of PHD finger protein 24
1wil A 32 A 35
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 147 and 150 (32 and 35 respectively in this structure).
Details
Redox score ?
78
PDB code
1wil
Structure name
solution structure of the ring finger domain of the human kiaa1045 protein
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
6
Peptide accession
Q9UPV7
Residue number A
147
Residue number B
150
Peptide name
PHD finger protein 24
Ligandability
Cysteine 147 of PHD finger protein 24
Cysteine 150 of PHD finger protein 24
1wil A 32 A 73
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 147 and 188 (32 and 73 respectively in this structure).
Details
Redox score ?
78
PDB code
1wil
Structure name
solution structure of the ring finger domain of the human kiaa1045 protein
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
8
% buried
5
Peptide accession
Q9UPV7
Residue number A
147
Residue number B
188
Peptide name
PHD finger protein 24
Ligandability
Cysteine 147 of PHD finger protein 24
Cysteine 188 of PHD finger protein 24
1wil A 32 A 70
A redox-regulated disulphide may form within PHD finger protein 24 between cysteines 147 and 185 (32 and 70 respectively in this structure).
Details
Redox score ?
77
PDB code
1wil
Structure name
solution structure of the ring finger domain of the human kiaa1045 protein
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
9
% buried
9
Peptide accession
Q9UPV7
Residue number A
147
Residue number B
185
Peptide name
PHD finger protein 24
Ligandability
Cysteine 147 of PHD finger protein 24
Cysteine 185 of PHD finger protein 24
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