Actin-binding LIM protein 2
Intramolecular
Cysteine 238 and cysteine 241
Cysteine 109 and cysteine 134
Cysteine 109 and cysteine 112
Cysteine 212 and cysteine 215
Cysteine 109 and cysteine 131
Cysteine 238 and cysteine 263
Cysteine 83 and cysteine 86
Cysteine 212 and cysteine 235
Cysteine 83 and cysteine 106
Cysteine 131 and cysteine 134
More...Cysteine 112 and cysteine 131
Cysteine 241 and cysteine 263
Cysteine 112 and cysteine 134
Cysteine 215 and cysteine 235
Cysteine 86 and cysteine 106
Cysteine 109 and cysteine 129
Cysteine 129 and cysteine 131
Cysteine 112 and cysteine 129
Cysteine 106 and cysteine 129
1wig A 34 A 37
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 238 and 241 (34 and 37 respectively in this structure).
Details
Redox score ?
90
PDB code
1wig
Structure name
solution structure of rsgi ruh-019, a lim domain of actin binding lim protein 2 (kiaa1808 protein) from human cdna
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
3
Peptide accession
Q6H8Q1
Residue number A
238
Residue number B
241
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 238 of Actin-binding LIM protein 2
Cysteine 241 of Actin-binding LIM protein 2
1v6g A 44 A 69
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 109 and 134 (44 and 69 respectively in this structure).
Details
Redox score ?
89
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
0
Peptide accession
Q6H8Q1
Residue number A
109
Residue number B
134
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 109 of Actin-binding LIM protein 2
Cysteine 134 of Actin-binding LIM protein 2
1v6g A 44 A 47
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 109 and 112 (44 and 47 respectively in this structure).
Details
Redox score ?
89
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
5
% buried
0
Peptide accession
Q6H8Q1
Residue number A
109
Residue number B
112
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 109 of Actin-binding LIM protein 2
Cysteine 112 of Actin-binding LIM protein 2
1wig A 8 A 11
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 212 and 215 (8 and 11 respectively in this structure).
Details
Redox score ?
89
PDB code
1wig
Structure name
solution structure of rsgi ruh-019, a lim domain of actin binding lim protein 2 (kiaa1808 protein) from human cdna
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
5
% buried
0
Peptide accession
Q6H8Q1
Residue number A
212
Residue number B
215
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 212 of Actin-binding LIM protein 2
Cysteine 215 of Actin-binding LIM protein 2
1v6g A 44 A 66
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 109 and 131 (44 and 66 respectively in this structure).
Details
Redox score ?
88
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
0
Peptide accession
Q6H8Q1
Residue number A
109
Residue number B
131
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 109 of Actin-binding LIM protein 2
Cysteine 131 of Actin-binding LIM protein 2
1wig A 34 A 59
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 238 and 263 (34 and 59 respectively in this structure).
Details
Redox score ?
88
PDB code
1wig
Structure name
solution structure of rsgi ruh-019, a lim domain of actin binding lim protein 2 (kiaa1808 protein) from human cdna
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
3
Peptide accession
Q6H8Q1
Residue number A
238
Residue number B
263
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 238 of Actin-binding LIM protein 2
Cysteine 263 of Actin-binding LIM protein 2
1v6g A 18 A 21
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 83 and 86 (18 and 21 respectively in this structure).
Details
Redox score ?
86
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
6
% buried
0
Peptide accession
Q6H8Q1
Residue number A
83
Residue number B
86
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 83 of Actin-binding LIM protein 2
Cysteine 86 of Actin-binding LIM protein 2
1wig A 8 A 31
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 212 and 235 (8 and 31 respectively in this structure).
Details
Redox score ?
85
PDB code
1wig
Structure name
solution structure of rsgi ruh-019, a lim domain of actin binding lim protein 2 (kiaa1808 protein) from human cdna
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
0
Peptide accession
Q6H8Q1
Residue number A
212
Residue number B
235
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 212 of Actin-binding LIM protein 2
Cysteine 235 of Actin-binding LIM protein 2
1v6g A 18 A 41
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 83 and 106 (18 and 41 respectively in this structure).
Details
Redox score ?
84
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
6
% buried
2
Peptide accession
Q6H8Q1
Residue number A
83
Residue number B
106
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 83 of Actin-binding LIM protein 2
Cysteine 106 of Actin-binding LIM protein 2
1v6g A 66 A 69
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 131 and 134 (66 and 69 respectively in this structure).
Details
Redox score ?
83
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
0
Peptide accession
Q6H8Q1
Residue number A
131
Residue number B
134
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 131 of Actin-binding LIM protein 2
Cysteine 134 of Actin-binding LIM protein 2
1v6g A 47 A 66
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 112 and 131 (47 and 66 respectively in this structure).
Details
Redox score ?
82
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
7
% buried
0
Peptide accession
Q6H8Q1
Residue number A
112
Residue number B
131
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 112 of Actin-binding LIM protein 2
Cysteine 131 of Actin-binding LIM protein 2
1wig A 37 A 59
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 241 and 263 (37 and 59 respectively in this structure).
Details
Redox score ?
79
PDB code
1wig
Structure name
solution structure of rsgi ruh-019, a lim domain of actin binding lim protein 2 (kiaa1808 protein) from human cdna
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
38
Minimum pKa ?
8
% buried
0
Peptide accession
Q6H8Q1
Residue number A
241
Residue number B
263
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 241 of Actin-binding LIM protein 2
Cysteine 263 of Actin-binding LIM protein 2
1v6g A 47 A 69
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 112 and 134 (47 and 69 respectively in this structure).
Details
Redox score ?
76
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
10
% buried
0
Peptide accession
Q6H8Q1
Residue number A
112
Residue number B
134
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 112 of Actin-binding LIM protein 2
Cysteine 134 of Actin-binding LIM protein 2
1wig A 11 A 31
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 215 and 235 (11 and 31 respectively in this structure).
Details
Redox score ?
76
PDB code
1wig
Structure name
solution structure of rsgi ruh-019, a lim domain of actin binding lim protein 2 (kiaa1808 protein) from human cdna
Structure deposition date
2004-05-28
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
Q6H8Q1
Residue number A
215
Residue number B
235
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 215 of Actin-binding LIM protein 2
Cysteine 235 of Actin-binding LIM protein 2
1v6g A 21 A 41
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 86 and 106 (21 and 41 respectively in this structure).
Details
Redox score ?
75
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
41
Minimum pKa ?
10
% buried
2
Peptide accession
Q6H8Q1
Residue number A
86
Residue number B
106
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 86 of Actin-binding LIM protein 2
Cysteine 106 of Actin-binding LIM protein 2
1v6g A 44 A 64
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 109 and 129 (44 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
59
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
8
Peptide accession
Q6H8Q1
Residue number A
109
Residue number B
129
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 109 of Actin-binding LIM protein 2
Cysteine 129 of Actin-binding LIM protein 2
1v6g A 64 A 66
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 129 and 131 (64 and 66 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
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
52
Minimum pKa ?
7
% buried
8
Peptide accession
Q6H8Q1
Residue number A
129
Residue number B
131
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 129 of Actin-binding LIM protein 2
Cysteine 131 of Actin-binding LIM protein 2
1v6g A 47 A 64
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 112 and 129 (47 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
47
Minimum pKa ?
10
% buried
8
Peptide accession
Q6H8Q1
Residue number A
112
Residue number B
129
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 112 of Actin-binding LIM protein 2
Cysteine 129 of Actin-binding LIM protein 2
1v6g A 41 A 64
A redox-regulated disulphide may form within Actin-binding LIM protein 2 between cysteines 106 and 129 (41 and 64 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
1v6g
Structure name
solution structure of the lim domain of the human actin binding lim protein 2
Structure deposition date
2003-11-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
51
Minimum pKa ?
10
% buried
10
Peptide accession
Q6H8Q1
Residue number A
106
Residue number B
129
Peptide name
Actin-binding LIM protein 2
Ligandability
Cysteine 106 of Actin-binding LIM protein 2
Cysteine 129 of Actin-binding LIM protein 2
If this tool was useful for finding a disulphide, please cite: