P-selectin
Intramolecular
Cysteine 168 and cysteine 183
Cysteine 163 and cysteine 174
Cysteine 185 and cysteine 194
Cysteine 60 and cysteine 158
Cysteine 131 and cysteine 150
Cysteine 168 and cysteine 174
Cysteine 183 and cysteine 194
Cysteine 168 and cysteine 194
Cysteine 174 and cysteine 183
Cysteine 183 and cysteine 185
More...Cysteine 163 and cysteine 168
Cysteine 168 and cysteine 185
Cysteine 163 and cysteine 183
Cysteine 174 and cysteine 194
Cysteine 174 and cysteine 185
Cysteine 163 and cysteine 185
Cysteine 163 and cysteine 194
1g1q C 127 C 142
A redox-regulated disulphide may form within P-selectin between cysteines 168 and 183 (127 and 142 respectively in this structure).
Details
Redox score ?
88
PDB code
1g1q
Structure name
crystal structure of p-selectin lectin/egf domains
Structure deposition date
2000-10-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
168
Residue number B
183
Peptide name
P-selectin
Ligandability
Cysteine 168 of P-selectin
Cysteine 183 of P-selectin
1g1r D 122 D 133
A redox-regulated disulphide may form within P-selectin between cysteines 163 and 174 (122 and 133 respectively in this structure).
Details
Redox score ?
87
PDB code
1g1r
Structure name
crystal structure of p-selectin lectin/egf domains complexed with slex
Structure deposition date
2000-10-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
58
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
163
Residue number B
174
Peptide name
P-selectin
Ligandability
Cysteine 163 of P-selectin
Cysteine 174 of P-selectin
1g1r D 144 D 153
A redox-regulated disulphide may form within P-selectin between cysteines 185 and 194 (144 and 153 respectively in this structure).
Details
Redox score ?
86
PDB code
1g1r
Structure name
crystal structure of p-selectin lectin/egf domains complexed with slex
Structure deposition date
2000-10-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
185
Residue number B
194
Peptide name
P-selectin
Ligandability
Cysteine 185 of P-selectin
Cysteine 194 of P-selectin
1g1r B 19 B 117
A redox-regulated disulphide may form within P-selectin between cysteines 60 and 158 (19 and 117 respectively in this structure).
Details
Redox score ?
84
PDB code
1g1r
Structure name
crystal structure of p-selectin lectin/egf domains complexed with slex
Structure deposition date
2000-10-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
70
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
60
Residue number B
158
Peptide name
P-selectin
Ligandability
Cysteine 60 of P-selectin
Cysteine 158 of P-selectin
1g1q C 90 C 109
A redox-regulated disulphide may form within P-selectin between cysteines 131 and 150 (90 and 109 respectively in this structure).
Details
Redox score ?
83
PDB code
1g1q
Structure name
crystal structure of p-selectin lectin/egf domains
Structure deposition date
2000-10-13
Thiol separation (Å)
2
Half-sphere exposure sum ?
72
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
131
Residue number B
150
Peptide name
P-selectin
Ligandability
Cysteine 131 of P-selectin
Cysteine 150 of P-selectin
1g1r B 127 B 133
A redox-regulated disulphide may form within P-selectin between cysteines 168 and 174 (127 and 133 respectively in this structure).
Details
Redox score ?
74
PDB code
1g1r
Structure name
crystal structure of p-selectin lectin/egf domains complexed with slex
Structure deposition date
2000-10-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
168
Residue number B
174
Peptide name
P-selectin
Ligandability
Cysteine 168 of P-selectin
Cysteine 174 of P-selectin
1g1s B 142 B 153
A redox-regulated disulphide may form within P-selectin between cysteines 183 and 194 (142 and 153 respectively in this structure).
Details
Redox score ?
73
PDB code
1g1s
Structure name
p-selectin lectin/egf domains complexed with psgl-1 peptide
Structure deposition date
2000-10-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
183
Residue number B
194
Peptide name
P-selectin
Ligandability
Cysteine 183 of P-selectin
Cysteine 194 of P-selectin
1g1s B 127 B 153
A redox-regulated disulphide may form within P-selectin between cysteines 168 and 194 (127 and 153 respectively in this structure).
Details
Redox score ?
71
PDB code
1g1s
Structure name
p-selectin lectin/egf domains complexed with psgl-1 peptide
Structure deposition date
2000-10-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
168
Residue number B
194
Peptide name
P-selectin
Ligandability
Cysteine 168 of P-selectin
Cysteine 194 of P-selectin
1g1r D 133 D 142
A redox-regulated disulphide may form within P-selectin between cysteines 174 and 183 (133 and 142 respectively in this structure).
Details
Redox score ?
70
PDB code
1g1r
Structure name
crystal structure of p-selectin lectin/egf domains complexed with slex
Structure deposition date
2000-10-13
Thiol separation (Å)
5
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
174
Residue number B
183
Peptide name
P-selectin
Ligandability
Cysteine 174 of P-selectin
Cysteine 183 of P-selectin
1g1r D 142 D 144
A redox-regulated disulphide may form within P-selectin between cysteines 183 and 185 (142 and 144 respectively in this structure).
Details
Redox score ?
64
PDB code
1g1r
Structure name
crystal structure of p-selectin lectin/egf domains complexed with slex
Structure deposition date
2000-10-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
183
Residue number B
185
Peptide name
P-selectin
Ligandability
Cysteine 183 of P-selectin
Cysteine 185 of P-selectin
1g1q B 122 B 127
A redox-regulated disulphide may form within P-selectin between cysteines 163 and 168 (122 and 127 respectively in this structure).
Details
Redox score ?
62
PDB code
1g1q
Structure name
crystal structure of p-selectin lectin/egf domains
Structure deposition date
2000-10-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
56
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
163
Residue number B
168
Peptide name
P-selectin
Ligandability
Cysteine 163 of P-selectin
Cysteine 168 of P-selectin
1g1r A 127 A 144
A redox-regulated disulphide may form within P-selectin between cysteines 168 and 185 (127 and 144 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
1g1r
Structure name
crystal structure of p-selectin lectin/egf domains complexed with slex
Structure deposition date
2000-10-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
53
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
168
Residue number B
185
Peptide name
P-selectin
Ligandability
Cysteine 168 of P-selectin
Cysteine 185 of P-selectin
1g1r D 122 D 142
A redox-regulated disulphide may form within P-selectin between cysteines 163 and 183 (122 and 142 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
58
PDB code
1g1r
Structure name
crystal structure of p-selectin lectin/egf domains complexed with slex
Structure deposition date
2000-10-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
163
Residue number B
183
Peptide name
P-selectin
Ligandability
Cysteine 163 of P-selectin
Cysteine 183 of P-selectin
1g1s B 133 B 153
A redox-regulated disulphide may form within P-selectin between cysteines 174 and 194 (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 ?
47
PDB code
1g1s
Structure name
p-selectin lectin/egf domains complexed with psgl-1 peptide
Structure deposition date
2000-10-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
174
Residue number B
194
Peptide name
P-selectin
Ligandability
Cysteine 174 of P-selectin
Cysteine 194 of P-selectin
1fsb A 15 A 26
A redox-regulated disulphide may form within P-selectin between cysteines 174 and 185 (15 and 26 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
1fsb
Structure name
structure of the egf domain of p-selectin, nmr, 19 structures
Structure deposition date
1996-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
51
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
174
Residue number B
185
Peptide name
P-selectin
Ligandability
Cysteine 174 of P-selectin
Cysteine 185 of P-selectin
1fsb A 4 A 26
A redox-regulated disulphide may form within P-selectin between cysteines 163 and 185 (4 and 26 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
1fsb
Structure name
structure of the egf domain of p-selectin, nmr, 19 structures
Structure deposition date
1996-03-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
163
Residue number B
185
Peptide name
P-selectin
Ligandability
Cysteine 163 of P-selectin
Cysteine 185 of P-selectin
1fsb A 4 A 35
A redox-regulated disulphide may form within P-selectin between cysteines 163 and 194 (4 and 35 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
1fsb
Structure name
structure of the egf domain of p-selectin, nmr, 19 structures
Structure deposition date
1996-03-25
Thiol separation (Å)
10
Half-sphere exposure sum ?
48
Minimum pKa ?
nan
% buried
nan
Peptide accession
P16109
Residue number A
163
Residue number B
194
Peptide name
P-selectin
Ligandability
Cysteine 163 of P-selectin
Cysteine 194 of P-selectin
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