Polycomb group RING finger protein 6
Intramolecular
Cysteine 134 and cysteine 137
Cysteine 134 and cysteine 155
Cysteine 134 and cysteine 158
Cysteine 150 and cysteine 169
Cysteine 150 and cysteine 172
Cysteine 169 and cysteine 172
Cysteine 137 and cysteine 158
Cysteine 137 and cysteine 155
Cysteine 155 and cysteine 158
Cysteine 134 and cysteine 169
Cysteine 158 and cysteine 169
2djb A 18 A 21
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 134 and 137 (18 and 21 respectively in this structure).
Details
Redox score ?
89
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
2
Peptide accession
Q9BYE7
Residue number A
134
Residue number B
137
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 134 of Polycomb group RING finger protein 6
Cysteine 137 of Polycomb group RING finger protein 6
2djb A 18 A 39
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 134 and 155 (18 and 39 respectively in this structure).
Details
Redox score ?
89
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
2
Peptide accession
Q9BYE7
Residue number A
134
Residue number B
155
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 134 of Polycomb group RING finger protein 6
Cysteine 155 of Polycomb group RING finger protein 6
2djb A 18 A 42
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 134 and 158 (18 and 42 respectively in this structure).
Details
Redox score ?
85
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
5
% buried
4
Peptide accession
Q9BYE7
Residue number A
134
Residue number B
158
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 134 of Polycomb group RING finger protein 6
Cysteine 158 of Polycomb group RING finger protein 6
2djb A 34 A 53
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 150 and 169 (34 and 53 respectively in this structure).
Details
Redox score ?
84
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
7
% buried
6
Peptide accession
Q9BYE7
Residue number A
150
Residue number B
169
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 150 of Polycomb group RING finger protein 6
Cysteine 169 of Polycomb group RING finger protein 6
2djb A 34 A 56
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 150 and 172 (34 and 56 respectively in this structure).
Details
Redox score ?
83
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
34
Minimum pKa ?
9
% buried
0
Peptide accession
Q9BYE7
Residue number A
150
Residue number B
172
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 150 of Polycomb group RING finger protein 6
Cysteine 172 of Polycomb group RING finger protein 6
2djb A 53 A 56
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 169 and 172 (53 and 56 respectively in this structure).
Details
Redox score ?
83
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
7
% buried
6
Peptide accession
Q9BYE7
Residue number A
169
Residue number B
172
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 169 of Polycomb group RING finger protein 6
Cysteine 172 of Polycomb group RING finger protein 6
2djb A 21 A 42
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 137 and 158 (21 and 42 respectively in this structure).
Details
Redox score ?
81
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
3
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
2
Peptide accession
Q9BYE7
Residue number A
137
Residue number B
158
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 137 of Polycomb group RING finger protein 6
Cysteine 158 of Polycomb group RING finger protein 6
2djb A 21 A 39
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 137 and 155 (21 and 39 respectively in this structure).
Details
Redox score ?
80
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BYE7
Residue number A
137
Residue number B
155
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 137 of Polycomb group RING finger protein 6
Cysteine 155 of Polycomb group RING finger protein 6
2djb A 39 A 42
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 155 and 158 (39 and 42 respectively in this structure).
Details
Redox score ?
72
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
10
% buried
2
Peptide accession
Q9BYE7
Residue number A
155
Residue number B
158
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 155 of Polycomb group RING finger protein 6
Cysteine 158 of Polycomb group RING finger protein 6
2djb A 18 A 53
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 134 and 169 (18 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
56
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
9
Peptide accession
Q9BYE7
Residue number A
134
Residue number B
169
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 134 of Polycomb group RING finger protein 6
Cysteine 169 of Polycomb group RING finger protein 6
2djb A 42 A 53
A redox-regulated disulphide may form within Polycomb group RING finger protein 6 between cysteines 158 and 169 (42 and 53 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
2djb
Structure name
solution structure of the ring domain of the human polycomb group ring finger protein 6
Structure deposition date
2006-03-31
Thiol separation (Å)
9
Half-sphere exposure sum ?
61
Minimum pKa ?
7
% buried
8
Peptide accession
Q9BYE7
Residue number A
158
Residue number B
169
Peptide name
Polycomb group RING finger protein 6
Ligandability
Cysteine 158 of Polycomb group RING finger protein 6
Cysteine 169 of Polycomb group RING finger protein 6
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