Fibrillin-1
Intramolecular
Cysteine 862 and cysteine 887
Cysteine 2070 and cysteine 2096
Cysteine 2131 and cysteine 2142
Cysteine 2192 and cysteine 2204
Cysteine 119 and cysteine 129
Cysteine 937 and cysteine 950
Cysteine 921 and cysteine 935
Cysteine 273 and cysteine 286
Cysteine 811 and cysteine 821
Cysteine 2153 and cysteine 2164
More...Cysteine 136 and cysteine 145
Cysteine 1074 and cysteine 1086
Cysteine 89 and cysteine 100
Cysteine 896 and cysteine 908
Cysteine 168 and cysteine 177
Cysteine 257 and cysteine 271
Cysteine 1491 and cysteine 1502
Cysteine 1633 and cysteine 1646
Cysteine 154 and cysteine 166
Cysteine 195 and cysteine 221
Cysteine 1549 and cysteine 1574
Cysteine 1081 and cysteine 1095
Cysteine 1140 and cysteine 1153
Cysteine 1097 and cysteine 1111
Cysteine 85 and cysteine 94
Cysteine 67 and cysteine 80
Cysteine 2176 and cysteine 2190
Cysteine 2170 and cysteine 2181
Cysteine 123 and cysteine 134
Cysteine 1117 and cysteine 1129
Cysteine 231 and cysteine 244
Cysteine 1497 and cysteine 1511
Cysteine 102 and cysteine 111
Cysteine 2137 and cysteine 2151
Cysteine 150 and cysteine 160
Cysteine 832 and cysteine 845
Cysteine 816 and cysteine 830
Cysteine 1610 and cysteine 1622
Cysteine 1124 and cysteine 1138
Cysteine 250 and cysteine 262
2w86 A 58 A 83
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 862 and 887 (58 and 83 respectively in this structure).
Details
Redox score ?
91
PDB code
2w86
Structure name
crystal structure of fibrillin-1 domains cbegf9hyb2cbegf10, calcium saturated form
Structure deposition date
2009-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
862
Residue number B
887
Peptide name
Fibrillin-1
Ligandability
Cysteine 862 of Fibrillin-1
Cysteine 887 of Fibrillin-1
1apj A 2070 A 2096
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 2070 and 2096.
Details
Redox score ?
90
PDB code
1apj
Structure name
nmr study of the transforming growth factor beta binding protein-like domain (tb module/8-cys domain), nmr, 21 structures
Structure deposition date
1997-07-22
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
2070
Residue number B
2096
Peptide name
Fibrillin-1
Ligandability
Cysteine 2070 of Fibrillin-1
Cysteine 2096 of Fibrillin-1
1emo A 2131 A 2142
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 2131 and 2142.
Details
Redox score ?
90
PDB code
1emo
Structure name
nmr study of a pair of fibrillin ca2+ binding epidermal growth factor- like domains, 22 structures
Structure deposition date
1996-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
2131
Residue number B
2142
Peptide name
Fibrillin-1
Ligandability
Cysteine 2131 of Fibrillin-1
Cysteine 2142 of Fibrillin-1
1emn A 2192 A 2204
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 2192 and 2204.
Details
Redox score ?
89
PDB code
1emn
Structure name
nmr study of a pair of fibrillin ca2+ binding epidermal growth factor- like domains, minimized average structure
Structure deposition date
1996-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
2192
Residue number B
2204
Peptide name
Fibrillin-1
Ligandability
Cysteine 2192 of Fibrillin-1
Cysteine 2204 of Fibrillin-1
5ms9 A 119 A 129
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 119 and 129.
Details
Redox score ?
89
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
41
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
119
Residue number B
129
Peptide name
Fibrillin-1
Ligandability
Cysteine 119 of Fibrillin-1
Cysteine 129 of Fibrillin-1
2w86 A 133 A 146
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 937 and 950 (133 and 146 respectively in this structure).
Details
Redox score ?
89
PDB code
2w86
Structure name
crystal structure of fibrillin-1 domains cbegf9hyb2cbegf10, calcium saturated form
Structure deposition date
2009-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
937
Residue number B
950
Peptide name
Fibrillin-1
Ligandability
Cysteine 937 of Fibrillin-1
Cysteine 950 of Fibrillin-1
2w86 A 117 A 131
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 921 and 935 (117 and 131 respectively in this structure).
Details
Redox score ?
88
PDB code
2w86
Structure name
crystal structure of fibrillin-1 domains cbegf9hyb2cbegf10, calcium saturated form
Structure deposition date
2009-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
921
Residue number B
935
Peptide name
Fibrillin-1
Ligandability
Cysteine 921 of Fibrillin-1
Cysteine 935 of Fibrillin-1
5ms9 A 273 A 286
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 273 and 286.
Details
Redox score ?
88
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
46
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
273
Residue number B
286
Peptide name
Fibrillin-1
Ligandability
Cysteine 273 of Fibrillin-1
Cysteine 286 of Fibrillin-1
2w86 A 7 A 17
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 811 and 821 (7 and 17 respectively in this structure).
Details
Redox score ?
88
PDB code
2w86
Structure name
crystal structure of fibrillin-1 domains cbegf9hyb2cbegf10, calcium saturated form
Structure deposition date
2009-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
811
Residue number B
821
Peptide name
Fibrillin-1
Ligandability
Cysteine 811 of Fibrillin-1
Cysteine 821 of Fibrillin-1
1emo A 2153 A 2164
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 2153 and 2164.
Details
Redox score ?
88
PDB code
1emo
Structure name
nmr study of a pair of fibrillin ca2+ binding epidermal growth factor- like domains, 22 structures
Structure deposition date
1996-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
2153
Residue number B
2164
Peptide name
Fibrillin-1
Ligandability
Cysteine 2153 of Fibrillin-1
Cysteine 2164 of Fibrillin-1
5ms9 A 136 A 145
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 136 and 145.
Details
Redox score ?
88
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
136
Residue number B
145
Peptide name
Fibrillin-1
Ligandability
Cysteine 136 of Fibrillin-1
Cysteine 145 of Fibrillin-1
1lmj A 8 A 20
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1074 and 1086 (8 and 20 respectively in this structure).
Details
Redox score ?
88
PDB code
1lmj
Structure name
nmr study of the fibrillin-1 cbegf12-13 pair of ca2+ binding epidermal growth factor-like domains
Structure deposition date
2002-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1074
Residue number B
1086
Peptide name
Fibrillin-1
Ligandability
Cysteine 1074 of Fibrillin-1
Cysteine 1086 of Fibrillin-1
2m74 A 89 A 100
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 89 and 100.
Details
Redox score ?
87
PDB code
2m74
Structure name
1h, 13c and 15n assignments of the four n-terminal domains of human fibrillin-1
Structure deposition date
2013-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
89
Residue number B
100
Peptide name
Fibrillin-1
Ligandability
Cysteine 89 of Fibrillin-1
Cysteine 100 of Fibrillin-1
2w86 A 92 A 104
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 896 and 908 (92 and 104 respectively in this structure).
Details
Redox score ?
87
PDB code
2w86
Structure name
crystal structure of fibrillin-1 domains cbegf9hyb2cbegf10, calcium saturated form
Structure deposition date
2009-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
896
Residue number B
908
Peptide name
Fibrillin-1
Ligandability
Cysteine 896 of Fibrillin-1
Cysteine 908 of Fibrillin-1
5ms9 A 168 A 177
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 168 and 177.
Details
Redox score ?
87
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
168
Residue number B
177
Peptide name
Fibrillin-1
Ligandability
Cysteine 168 of Fibrillin-1
Cysteine 177 of Fibrillin-1
5ms9 A 257 A 271
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 257 and 271.
Details
Redox score ?
87
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
257
Residue number B
271
Peptide name
Fibrillin-1
Ligandability
Cysteine 257 of Fibrillin-1
Cysteine 271 of Fibrillin-1
1uzj C 3491 C 3502
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1491 and 1502 (3491 and 3502 respectively in this structure).
Details
Redox score ?
87
PDB code
1uzj
Structure name
integrin binding cbegf22-tb4-cbegf33 fragment of human fibrillin-1, holo form
Structure deposition date
2004-03-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1491
Residue number B
1502
Peptide name
Fibrillin-1
Ligandability
Cysteine 1491 of Fibrillin-1
Cysteine 1502 of Fibrillin-1
1uzj C 3633 C 3646
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1633 and 1646 (3633 and 3646 respectively in this structure).
Details
Redox score ?
87
PDB code
1uzj
Structure name
integrin binding cbegf22-tb4-cbegf33 fragment of human fibrillin-1, holo form
Structure deposition date
2004-03-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1633
Residue number B
1646
Peptide name
Fibrillin-1
Ligandability
Cysteine 1633 of Fibrillin-1
Cysteine 1646 of Fibrillin-1
2m74 A 154 A 166
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 154 and 166.
Details
Redox score ?
87
PDB code
2m74
Structure name
1h, 13c and 15n assignments of the four n-terminal domains of human fibrillin-1
Structure deposition date
2013-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
154
Residue number B
166
Peptide name
Fibrillin-1
Ligandability
Cysteine 154 of Fibrillin-1
Cysteine 166 of Fibrillin-1
5ms9 A 195 A 221
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 195 and 221.
Details
Redox score ?
87
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
195
Residue number B
221
Peptide name
Fibrillin-1
Ligandability
Cysteine 195 of Fibrillin-1
Cysteine 221 of Fibrillin-1
1uzj B 2549 B 2574
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1549 and 1574 (2549 and 2574 respectively in this structure).
Details
Redox score ?
87
PDB code
1uzj
Structure name
integrin binding cbegf22-tb4-cbegf33 fragment of human fibrillin-1, holo form
Structure deposition date
2004-03-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
59
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1549
Residue number B
1574
Peptide name
Fibrillin-1
Ligandability
Cysteine 1549 of Fibrillin-1
Cysteine 1574 of Fibrillin-1
1lmj A 15 A 29
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1081 and 1095 (15 and 29 respectively in this structure).
Details
Redox score ?
87
PDB code
1lmj
Structure name
nmr study of the fibrillin-1 cbegf12-13 pair of ca2+ binding epidermal growth factor-like domains
Structure deposition date
2002-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1081
Residue number B
1095
Peptide name
Fibrillin-1
Ligandability
Cysteine 1081 of Fibrillin-1
Cysteine 1095 of Fibrillin-1
1lmj A 74 A 87
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1140 and 1153 (74 and 87 respectively in this structure).
Details
Redox score ?
87
PDB code
1lmj
Structure name
nmr study of the fibrillin-1 cbegf12-13 pair of ca2+ binding epidermal growth factor-like domains
Structure deposition date
2002-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1140
Residue number B
1153
Peptide name
Fibrillin-1
Ligandability
Cysteine 1140 of Fibrillin-1
Cysteine 1153 of Fibrillin-1
1lmj A 31 A 45
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1097 and 1111 (31 and 45 respectively in this structure).
Details
Redox score ?
87
PDB code
1lmj
Structure name
nmr study of the fibrillin-1 cbegf12-13 pair of ca2+ binding epidermal growth factor-like domains
Structure deposition date
2002-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1097
Residue number B
1111
Peptide name
Fibrillin-1
Ligandability
Cysteine 1097 of Fibrillin-1
Cysteine 1111 of Fibrillin-1
2m74 A 85 A 94
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 85 and 94.
Details
Redox score ?
87
PDB code
2m74
Structure name
1h, 13c and 15n assignments of the four n-terminal domains of human fibrillin-1
Structure deposition date
2013-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
85
Residue number B
94
Peptide name
Fibrillin-1
Ligandability
Cysteine 85 of Fibrillin-1
Cysteine 94 of Fibrillin-1
2m74 A 67 A 80
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 67 and 80.
Details
Redox score ?
87
PDB code
2m74
Structure name
1h, 13c and 15n assignments of the four n-terminal domains of human fibrillin-1
Structure deposition date
2013-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
67
Residue number B
80
Peptide name
Fibrillin-1
Ligandability
Cysteine 67 of Fibrillin-1
Cysteine 80 of Fibrillin-1
1emn A 2176 A 2190
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 2176 and 2190.
Details
Redox score ?
87
PDB code
1emn
Structure name
nmr study of a pair of fibrillin ca2+ binding epidermal growth factor- like domains, minimized average structure
Structure deposition date
1996-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
2176
Residue number B
2190
Peptide name
Fibrillin-1
Ligandability
Cysteine 2176 of Fibrillin-1
Cysteine 2190 of Fibrillin-1
1emn A 2170 A 2181
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 2170 and 2181.
Details
Redox score ?
87
PDB code
1emn
Structure name
nmr study of a pair of fibrillin ca2+ binding epidermal growth factor- like domains, minimized average structure
Structure deposition date
1996-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
2170
Residue number B
2181
Peptide name
Fibrillin-1
Ligandability
Cysteine 2170 of Fibrillin-1
Cysteine 2181 of Fibrillin-1
2m74 A 123 A 134
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 123 and 134.
Details
Redox score ?
87
PDB code
2m74
Structure name
1h, 13c and 15n assignments of the four n-terminal domains of human fibrillin-1
Structure deposition date
2013-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
123
Residue number B
134
Peptide name
Fibrillin-1
Ligandability
Cysteine 123 of Fibrillin-1
Cysteine 134 of Fibrillin-1
1lmj A 51 A 63
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1117 and 1129 (51 and 63 respectively in this structure).
Details
Redox score ?
87
PDB code
1lmj
Structure name
nmr study of the fibrillin-1 cbegf12-13 pair of ca2+ binding epidermal growth factor-like domains
Structure deposition date
2002-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1117
Residue number B
1129
Peptide name
Fibrillin-1
Ligandability
Cysteine 1117 of Fibrillin-1
Cysteine 1129 of Fibrillin-1
5ms9 A 231 A 244
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 231 and 244.
Details
Redox score ?
87
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
44
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
231
Residue number B
244
Peptide name
Fibrillin-1
Ligandability
Cysteine 231 of Fibrillin-1
Cysteine 244 of Fibrillin-1
1uzj A 1497 A 1511
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1497 and 1511.
Details
Redox score ?
87
PDB code
1uzj
Structure name
integrin binding cbegf22-tb4-cbegf33 fragment of human fibrillin-1, holo form
Structure deposition date
2004-03-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1497
Residue number B
1511
Peptide name
Fibrillin-1
Ligandability
Cysteine 1497 of Fibrillin-1
Cysteine 1511 of Fibrillin-1
2m74 A 102 A 111
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 102 and 111.
Details
Redox score ?
86
PDB code
2m74
Structure name
1h, 13c and 15n assignments of the four n-terminal domains of human fibrillin-1
Structure deposition date
2013-04-17
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
102
Residue number B
111
Peptide name
Fibrillin-1
Ligandability
Cysteine 102 of Fibrillin-1
Cysteine 111 of Fibrillin-1
1emn A 2137 A 2151
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 2137 and 2151.
Details
Redox score ?
86
PDB code
1emn
Structure name
nmr study of a pair of fibrillin ca2+ binding epidermal growth factor- like domains, minimized average structure
Structure deposition date
1996-08-05
Thiol separation (Å)
2
Half-sphere exposure sum ?
61
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
2137
Residue number B
2151
Peptide name
Fibrillin-1
Ligandability
Cysteine 2137 of Fibrillin-1
Cysteine 2151 of Fibrillin-1
5ms9 A 150 A 160
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 150 and 160.
Details
Redox score ?
86
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
150
Residue number B
160
Peptide name
Fibrillin-1
Ligandability
Cysteine 150 of Fibrillin-1
Cysteine 160 of Fibrillin-1
2w86 A 28 A 41
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 832 and 845 (28 and 41 respectively in this structure).
Details
Redox score ?
86
PDB code
2w86
Structure name
crystal structure of fibrillin-1 domains cbegf9hyb2cbegf10, calcium saturated form
Structure deposition date
2009-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
832
Residue number B
845
Peptide name
Fibrillin-1
Ligandability
Cysteine 832 of Fibrillin-1
Cysteine 845 of Fibrillin-1
2w86 A 12 A 26
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 816 and 830 (12 and 26 respectively in this structure).
Details
Redox score ?
86
PDB code
2w86
Structure name
crystal structure of fibrillin-1 domains cbegf9hyb2cbegf10, calcium saturated form
Structure deposition date
2009-01-09
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
816
Residue number B
830
Peptide name
Fibrillin-1
Ligandability
Cysteine 816 of Fibrillin-1
Cysteine 830 of Fibrillin-1
1uzj A 1610 A 1622
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1610 and 1622.
Details
Redox score ?
86
PDB code
1uzj
Structure name
integrin binding cbegf22-tb4-cbegf33 fragment of human fibrillin-1, holo form
Structure deposition date
2004-03-12
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1610
Residue number B
1622
Peptide name
Fibrillin-1
Ligandability
Cysteine 1610 of Fibrillin-1
Cysteine 1622 of Fibrillin-1
1lmj A 58 A 72
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 1124 and 1138 (58 and 72 respectively in this structure).
Details
Redox score ?
86
PDB code
1lmj
Structure name
nmr study of the fibrillin-1 cbegf12-13 pair of ca2+ binding epidermal growth factor-like domains
Structure deposition date
2002-05-02
Thiol separation (Å)
2
Half-sphere exposure sum ?
64
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
1124
Residue number B
1138
Peptide name
Fibrillin-1
Ligandability
Cysteine 1124 of Fibrillin-1
Cysteine 1138 of Fibrillin-1
5ms9 A 250 A 262
A redox-regulated disulphide may form within Fibrillin-1 between cysteines 250 and 262.
Details
Redox score ?
85
PDB code
5ms9
Structure name
solution structure of human fibrillin-1 egf2-egf3-hybrid1-cbegf1 four domain fragment
Structure deposition date
2017-01-01
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P35555
Residue number A
250
Residue number B
262
Peptide name
Fibrillin-1
Ligandability
Cysteine 250 of Fibrillin-1
Cysteine 262 of Fibrillin-1
If this tool was useful for finding a disulphide, please cite: