L-selectin
Intramolecular
Cysteine 182 and cysteine 191
Cysteine 165 and cysteine 180
Cysteine 160 and cysteine 171
Cysteine 57 and cysteine 155
Cysteine 128 and cysteine 147
Cysteine 180 and cysteine 191
Cysteine 165 and cysteine 171
Cysteine 171 and cysteine 180
Cysteine 165 and cysteine 191
Cysteine 165 and cysteine 182
More...Cysteine 180 and cysteine 182
Cysteine 160 and cysteine 180
Cysteine 160 and cysteine 165
Cysteine 171 and cysteine 191
5vc1 A 144 A 153
A redox-regulated disulphide may form within L-selectin between cysteines 182 and 191 (144 and 153 respectively in this structure).
Details
Redox score ?
91
PDB code
5vc1
Structure name
crystal structure of l-selectin lectin/egf domains
Structure deposition date
2017-03-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
nan
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
182
Residue number B
191
Peptide name
L-selectin
Ligandability
Cysteine 182 of L-selectin
Cysteine 191 of L-selectin
3cfw A 127 A 142
A redox-regulated disulphide may form within L-selectin between cysteines 165 and 180 (127 and 142 respectively in this structure).
Details
Redox score ?
88
PDB code
3cfw
Structure name
l-selectin lectin and egf domains
Structure deposition date
2008-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
165
Residue number B
180
Peptide name
L-selectin
Ligandability
Cysteine 165 of L-selectin
Cysteine 180 of L-selectin
5vc1 A 122 A 133
A redox-regulated disulphide may form within L-selectin between cysteines 160 and 171 (122 and 133 respectively in this structure).
Details
Redox score ?
87
PDB code
5vc1
Structure name
crystal structure of l-selectin lectin/egf domains
Structure deposition date
2017-03-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
160
Residue number B
171
Peptide name
L-selectin
Ligandability
Cysteine 160 of L-selectin
Cysteine 171 of L-selectin
5vc1 A 19 A 117
A redox-regulated disulphide may form within L-selectin between cysteines 57 and 155 (19 and 117 respectively in this structure).
Details
Redox score ?
84
PDB code
5vc1
Structure name
crystal structure of l-selectin lectin/egf domains
Structure deposition date
2017-03-30
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
57
Residue number B
155
Peptide name
L-selectin
Ligandability
Cysteine 57 of L-selectin
Cysteine 155 of L-selectin
3cfw A 90 A 109
A redox-regulated disulphide may form within L-selectin between cysteines 128 and 147 (90 and 109 respectively in this structure).
Details
Redox score ?
82
PDB code
3cfw
Structure name
l-selectin lectin and egf domains
Structure deposition date
2008-03-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
128
Residue number B
147
Peptide name
L-selectin
Ligandability
Cysteine 128 of L-selectin
Cysteine 147 of L-selectin
3cfw A 142 A 153
A redox-regulated disulphide may form within L-selectin between cysteines 180 and 191 (142 and 153 respectively in this structure).
Details
Redox score ?
75
PDB code
3cfw
Structure name
l-selectin lectin and egf domains
Structure deposition date
2008-03-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
180
Residue number B
191
Peptide name
L-selectin
Ligandability
Cysteine 180 of L-selectin
Cysteine 191 of L-selectin
3cfw A 127 A 133
A redox-regulated disulphide may form within L-selectin between cysteines 165 and 171 (127 and 133 respectively in this structure).
Details
Redox score ?
74
PDB code
3cfw
Structure name
l-selectin lectin and egf domains
Structure deposition date
2008-03-04
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
165
Residue number B
171
Peptide name
L-selectin
Ligandability
Cysteine 165 of L-selectin
Cysteine 171 of L-selectin
5vc1 A 133 A 142
A redox-regulated disulphide may form within L-selectin between cysteines 171 and 180 (133 and 142 respectively in this structure).
Details
Redox score ?
74
PDB code
5vc1
Structure name
crystal structure of l-selectin lectin/egf domains
Structure deposition date
2017-03-30
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
171
Residue number B
180
Peptide name
L-selectin
Ligandability
Cysteine 171 of L-selectin
Cysteine 180 of L-selectin
3cfw A 127 A 153
A redox-regulated disulphide may form within L-selectin between cysteines 165 and 191 (127 and 153 respectively in this structure).
Details
Redox score ?
69
PDB code
3cfw
Structure name
l-selectin lectin and egf domains
Structure deposition date
2008-03-04
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
165
Residue number B
191
Peptide name
L-selectin
Ligandability
Cysteine 165 of L-selectin
Cysteine 191 of L-selectin
5vc1 A 127 A 144
A redox-regulated disulphide may form within L-selectin between cysteines 165 and 182 (127 and 144 respectively in this structure).
Details
Redox score ?
63
PDB code
5vc1
Structure name
crystal structure of l-selectin lectin/egf domains
Structure deposition date
2017-03-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
47
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
165
Residue number B
182
Peptide name
L-selectin
Ligandability
Cysteine 165 of L-selectin
Cysteine 182 of L-selectin
5vc1 A 142 A 144
A redox-regulated disulphide may form within L-selectin between cysteines 180 and 182 (142 and 144 respectively in this structure).
Details
Redox score ?
63
PDB code
5vc1
Structure name
crystal structure of l-selectin lectin/egf domains
Structure deposition date
2017-03-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
180
Residue number B
182
Peptide name
L-selectin
Ligandability
Cysteine 180 of L-selectin
Cysteine 182 of L-selectin
5vc1 A 122 A 142
A redox-regulated disulphide may form within L-selectin between cysteines 160 and 180 (122 and 142 respectively in this structure).
Details
Redox score ?
63
PDB code
5vc1
Structure name
crystal structure of l-selectin lectin/egf domains
Structure deposition date
2017-03-30
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
160
Residue number B
180
Peptide name
L-selectin
Ligandability
Cysteine 160 of L-selectin
Cysteine 180 of L-selectin
3cfw A 122 A 127
A redox-regulated disulphide may form within L-selectin between cysteines 160 and 165 (122 and 127 respectively in this structure).
Details
Redox score ?
62
PDB code
3cfw
Structure name
l-selectin lectin and egf domains
Structure deposition date
2008-03-04
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
160
Residue number B
165
Peptide name
L-selectin
Ligandability
Cysteine 160 of L-selectin
Cysteine 165 of L-selectin
3cfw A 133 A 153
A redox-regulated disulphide may form within L-selectin between cysteines 171 and 191 (133 and 153 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
3cfw
Structure name
l-selectin lectin and egf domains
Structure deposition date
2008-03-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
50
Minimum pKa ?
nan
% buried
nan
Peptide accession
P14151
Residue number A
171
Residue number B
191
Peptide name
L-selectin
Ligandability
Cysteine 171 of L-selectin
Cysteine 191 of L-selectin
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