Four and a half LIM domains protein 3
Intramolecular
Cysteine 188 and cysteine 212
Cysteine 101 and cysteine 104
Cysteine 188 and cysteine 191
Cysteine 129 and cysteine 153 L
Cysteine 101 and cysteine 126
Cysteine 68 and cysteine 92
Cysteine 68 and cysteine 71
Cysteine 68 and cysteine 89
Cysteine 40 and cysteine 43
Cysteine 188 and cysteine 209
More...Cysteine 162 and cysteine 165
Cysteine 162 and cysteine 185
Cysteine 129 and cysteine 132
Cysteine 129 and cysteine 150
Cysteine 40 and cysteine 65 L
Cysteine 150 and cysteine 153 L
Cysteine 191 and cysteine 209
Cysteine 71 and cysteine 89
Cysteine 89 and cysteine 92
Cysteine 132 and cysteine 150
Cysteine 71 and cysteine 92
Cysteine 209 and cysteine 212
Cysteine 43 and cysteine 65 L
Cysteine 165 and cysteine 185
Cysteine 104 and cysteine 126
Cysteine 132 and cysteine 153 L
Cysteine 191 and cysteine 212
Cysteine 68 and cysteine 69
Cysteine 92 and cysteine 94
Cysteine 89 and cysteine 94
Cysteine 69 and cysteine 89
Cysteine 69 and cysteine 71
Cysteine 69 and cysteine 92
Cysteine 69 and cysteine 82
2cuq A 44 A 68
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 188 and 212 (44 and 68 respectively in this structure).
Details
Redox score ?
91
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
2
Peptide accession
Q13643
Residue number A
188
Residue number B
212
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 188 of Four and a half LIM domains protein 3
Cysteine 212 of Four and a half LIM domains protein 3
1wyh A 8 A 11
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 101 and 104 (8 and 11 respectively in this structure).
Details
Redox score ?
91
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
40
Minimum pKa ?
4
% buried
1
Peptide accession
Q13643
Residue number A
101
Residue number B
104
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 101 of Four and a half LIM domains protein 3
Cysteine 104 of Four and a half LIM domains protein 3
2cuq A 44 A 47
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 188 and 191 (44 and 47 respectively in this structure).
Details
Redox score ?
89
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
46
Minimum pKa ?
5
% buried
2
Peptide accession
Q13643
Residue number A
188
Residue number B
191
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 188 of Four and a half LIM domains protein 3
Cysteine 191 of Four and a half LIM domains protein 3
1wyh A 36 A 60
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 129 and 153 (36 and 60 respectively in this structure).
Details
Redox score ?
89
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
3
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
2
Peptide accession
Q13643
Residue number A
129
Residue number B
153
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 129 of Four and a half LIM domains protein 3
Cysteine 153 of Four and a half LIM domains protein 3
1wyh A 8 A 33
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 101 and 126 (8 and 33 respectively in this structure).
Details
Redox score ?
89
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
4
% buried
1
Peptide accession
Q13643
Residue number A
101
Residue number B
126
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 101 of Four and a half LIM domains protein 3
Cysteine 126 of Four and a half LIM domains protein 3
2ehe A 46 A 70
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 68 and 92 (46 and 70 respectively in this structure).
Details
Redox score ?
89
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
2
Peptide accession
Q9BVA2
Residue number A
68
Residue number B
92
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 68 of Four and a half LIM domains protein 3
Cysteine 92 of Four and a half LIM domains protein 3
2ehe A 46 A 49
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 68 and 71 (46 and 49 respectively in this structure).
Details
Redox score ?
89
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
5
% buried
2
Peptide accession
Q9BVA2
Residue number A
68
Residue number B
71
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 68 of Four and a half LIM domains protein 3
Cysteine 71 of Four and a half LIM domains protein 3
2ehe A 46 A 67
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 68 and 89 (46 and 67 respectively in this structure).
Details
Redox score ?
89
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
5
% buried
2
Peptide accession
Q9BVA2
Residue number A
68
Residue number B
89
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 68 of Four and a half LIM domains protein 3
Cysteine 89 of Four and a half LIM domains protein 3
2ehe A 18 A 21
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 40 and 43 (18 and 21 respectively in this structure).
Details
Redox score ?
88
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
6
% buried
5
Peptide accession
Q9BVA2
Residue number A
40
Residue number B
43
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 40 of Four and a half LIM domains protein 3
Cysteine 43 of Four and a half LIM domains protein 3
2cuq A 44 A 65
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 188 and 209 (44 and 65 respectively in this structure).
Details
Redox score ?
87
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
2
Peptide accession
Q13643
Residue number A
188
Residue number B
209
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 188 of Four and a half LIM domains protein 3
Cysteine 209 of Four and a half LIM domains protein 3
2cuq A 18 A 21
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 162 and 165 (18 and 21 respectively in this structure).
Details
Redox score ?
87
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
5
% buried
2
Peptide accession
Q13643
Residue number A
162
Residue number B
165
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 162 of Four and a half LIM domains protein 3
Cysteine 165 of Four and a half LIM domains protein 3
2cuq A 18 A 41
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 162 and 185 (18 and 41 respectively in this structure).
Details
Redox score ?
86
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
52
Minimum pKa ?
5
% buried
2
Peptide accession
Q13643
Residue number A
162
Residue number B
185
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 162 of Four and a half LIM domains protein 3
Cysteine 185 of Four and a half LIM domains protein 3
1wyh A 36 A 39
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 129 and 132 (36 and 39 respectively in this structure).
Details
Redox score ?
86
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
49
Minimum pKa ?
6
% buried
2
Peptide accession
Q13643
Residue number A
129
Residue number B
132
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 129 of Four and a half LIM domains protein 3
Cysteine 132 of Four and a half LIM domains protein 3
1wyh A 36 A 57
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 129 and 150 (36 and 57 respectively in this structure).
Details
Redox score ?
86
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
59
Minimum pKa ?
6
% buried
2
Peptide accession
Q13643
Residue number A
129
Residue number B
150
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 129 of Four and a half LIM domains protein 3
Cysteine 150 of Four and a half LIM domains protein 3
2ehe A 18 A 43
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 40 and 65 (18 and 43 respectively in this structure).
Details
Redox score ?
85
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
6
% buried
8
Peptide accession
Q9BVA2
Residue number A
40
Residue number B
65
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 40 of Four and a half LIM domains protein 3
Cysteine 65 of Four and a half LIM domains protein 3
1wyh A 57 A 60
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 150 and 153 (57 and 60 respectively in this structure).
Details
Redox score ?
85
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
3
Half-sphere exposure sum ?
54
Minimum pKa ?
8
% buried
0
Peptide accession
Q13643
Residue number A
150
Residue number B
153
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 150 of Four and a half LIM domains protein 3
Cysteine 153 of Four and a half LIM domains protein 3
2cuq A 47 A 65
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 191 and 209 (47 and 65 respectively in this structure).
Details
Redox score ?
81
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
47
Minimum pKa ?
8
% buried
0
Peptide accession
Q13643
Residue number A
191
Residue number B
209
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 191 of Four and a half LIM domains protein 3
Cysteine 209 of Four and a half LIM domains protein 3
2ehe A 49 A 67
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 71 and 89 (49 and 67 respectively in this structure).
Details
Redox score ?
81
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
43
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BVA2
Residue number A
71
Residue number B
89
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 71 of Four and a half LIM domains protein 3
Cysteine 89 of Four and a half LIM domains protein 3
2ehe A 67 A 70
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 89 and 92 (67 and 70 respectively in this structure).
Details
Redox score ?
81
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
50
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BVA2
Residue number A
89
Residue number B
92
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 89 of Four and a half LIM domains protein 3
Cysteine 92 of Four and a half LIM domains protein 3
1wyh A 39 A 57
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 132 and 150 (39 and 57 respectively in this structure).
Details
Redox score ?
80
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
8
% buried
0
Peptide accession
Q13643
Residue number A
132
Residue number B
150
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 132 of Four and a half LIM domains protein 3
Cysteine 150 of Four and a half LIM domains protein 3
2ehe A 49 A 70
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 71 and 92 (49 and 70 respectively in this structure).
Details
Redox score ?
79
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
39
Minimum pKa ?
9
% buried
0
Peptide accession
Q9BVA2
Residue number A
71
Residue number B
92
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 71 of Four and a half LIM domains protein 3
Cysteine 92 of Four and a half LIM domains protein 3
2cuq A 65 A 68
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 209 and 212 (65 and 68 respectively in this structure).
Details
Redox score ?
79
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
8
% buried
0
Peptide accession
Q13643
Residue number A
209
Residue number B
212
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 209 of Four and a half LIM domains protein 3
Cysteine 212 of Four and a half LIM domains protein 3
2ehe A 21 A 43
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 43 and 65 (21 and 43 respectively in this structure).
Details
Redox score ?
78
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
9
% buried
4
Peptide accession
Q9BVA2
Residue number A
43
Residue number B
65
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 43 of Four and a half LIM domains protein 3
Cysteine 65 of Four and a half LIM domains protein 3
2cuq A 21 A 41
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 165 and 185 (21 and 41 respectively in this structure).
Details
Redox score ?
78
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
Q13643
Residue number A
165
Residue number B
185
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 165 of Four and a half LIM domains protein 3
Cysteine 185 of Four and a half LIM domains protein 3
1wyh A 11 A 33
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 104 and 126 (11 and 33 respectively in this structure).
Details
Redox score ?
77
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
42
Minimum pKa ?
9
% buried
0
Peptide accession
Q13643
Residue number A
104
Residue number B
126
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 104 of Four and a half LIM domains protein 3
Cysteine 126 of Four and a half LIM domains protein 3
1wyh A 39 A 60
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 132 and 153 (39 and 60 respectively in this structure).
Details
Redox score ?
76
PDB code
1wyh
Structure name
solution structure of the lim domain from human skeletal muscle lim- protein 2
Structure deposition date
2005-02-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
0
Peptide accession
Q13643
Residue number A
132
Residue number B
153
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 132 of Four and a half LIM domains protein 3
Cysteine 153 of Four and a half LIM domains protein 3
2cuq A 47 A 68
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 191 and 212 (47 and 68 respectively in this structure).
Details
Redox score ?
75
PDB code
2cuq
Structure name
solution structure of second lim domain from human skeletal muscle lim-protein 2
Structure deposition date
2005-05-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
44
Minimum pKa ?
10
% buried
0
Peptide accession
Q13643
Residue number A
191
Residue number B
212
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 191 of Four and a half LIM domains protein 3
Cysteine 212 of Four and a half LIM domains protein 3
2ehe A 46 A 47
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 68 and 69 (46 and 47 respectively in this structure).
Details
Redox score ?
67
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
7
Half-sphere exposure sum ?
50
Minimum pKa ?
5
% buried
4
Peptide accession
Q9BVA2
Residue number A
68
Residue number B
69
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 68 of Four and a half LIM domains protein 3
Cysteine 69 of Four and a half LIM domains protein 3
2ehe A 70 A 72
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 92 and 94 (70 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
0
Peptide accession
Q9BVA2
Residue number A
92
Residue number B
94
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 92 of Four and a half LIM domains protein 3
Cysteine 94 of Four and a half LIM domains protein 3
2ehe A 67 A 72
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 89 and 94 (67 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
42
Minimum pKa ?
8
% buried
0
Peptide accession
Q9BVA2
Residue number A
89
Residue number B
94
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 89 of Four and a half LIM domains protein 3
Cysteine 94 of Four and a half LIM domains protein 3
2ehe A 47 A 67
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 69 and 89 (47 and 67 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
49
Minimum pKa ?
8
% buried
3
Peptide accession
Q9BVA2
Residue number A
69
Residue number B
89
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 69 of Four and a half LIM domains protein 3
Cysteine 89 of Four and a half LIM domains protein 3
2ehe A 47 A 49
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 69 and 71 (47 and 49 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
38
Minimum pKa ?
9
% buried
3
Peptide accession
Q9BVA2
Residue number A
69
Residue number B
71
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 69 of Four and a half LIM domains protein 3
Cysteine 71 of Four and a half LIM domains protein 3
2ehe A 47 A 70
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 69 and 92 (47 and 70 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
43
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
45
Minimum pKa ?
10
% buried
3
Peptide accession
Q9BVA2
Residue number A
69
Residue number B
92
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 69 of Four and a half LIM domains protein 3
Cysteine 92 of Four and a half LIM domains protein 3
2ehe A 47 A 60
A redox-regulated disulphide may form within Four and a half LIM domains protein 3 between cysteines 69 and 82 (47 and 60 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
2ehe
Structure name
solution structure of the first lim domain from human four and a half lim domains protein 3
Structure deposition date
2007-03-06
Thiol separation (Å)
10
Half-sphere exposure sum ?
46
Minimum pKa ?
9
% buried
3
Peptide accession
Q9BVA2
Residue number A
69
Residue number B
82
Peptide name
Four and a half LIM domains protein 3
Ligandability
Cysteine 69 of Four and a half LIM domains protein 3
Cysteine 82 of Four and a half LIM domains protein 3
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