Lactotransferrin
Intramolecular
Cysteine 190 and cysteine 201
Cysteine 251 and cysteine 265
Cysteine 29 and cysteine 65
Cysteine 177 and cysteine 193
Cysteine 39 and cysteine 56
Cysteine 135 and cysteine 218
Cysteine 193 and cysteine 201
Cysteine 190 and cysteine 193
Cysteine 177 and cysteine 201
Cysteine 177 and cysteine 218
More...Cysteine 193 and cysteine 218
Cysteine 177 and cysteine 190
Cysteine 135 and cysteine 177
Cysteine 135 and cysteine 193
Cysteine 29 and cysteine 39
Cysteine 39 and cysteine 65
Cysteine 29 and cysteine 56
2pms A 171 A 182
A redox-regulated disulphide may form within Lactotransferrin between cysteines 190 and 201 (171 and 182 respectively in this structure).
Details
Redox score ?
82
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
190
Residue number B
201
Peptide name
Lactotransferrin
Ligandability
Cysteine 190 of Lactotransferrin
Cysteine 201 of Lactotransferrin
2pms A 232 A 246
A redox-regulated disulphide may form within Lactotransferrin between cysteines 251 and 265 (232 and 246 respectively in this structure).
Details
Redox score ?
81
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
65
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
251
Residue number B
265
Peptide name
Lactotransferrin
Ligandability
Cysteine 251 of Lactotransferrin
Cysteine 265 of Lactotransferrin
2pms B 10 B 46
A redox-regulated disulphide may form within Lactotransferrin between cysteines 29 and 65 (10 and 46 respectively in this structure).
Details
Redox score ?
80
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
29
Residue number B
65
Peptide name
Lactotransferrin
Ligandability
Cysteine 29 of Lactotransferrin
Cysteine 65 of Lactotransferrin
2pms B 158 B 174
A redox-regulated disulphide may form within Lactotransferrin between cysteines 177 and 193 (158 and 174 respectively in this structure).
Details
Redox score ?
80
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
97
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
177
Residue number B
193
Peptide name
Lactotransferrin
Ligandability
Cysteine 177 of Lactotransferrin
Cysteine 193 of Lactotransferrin
2pms B 20 B 37
A redox-regulated disulphide may form within Lactotransferrin between cysteines 39 and 56 (20 and 37 respectively in this structure).
Details
Redox score ?
79
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
39
Residue number B
56
Peptide name
Lactotransferrin
Ligandability
Cysteine 39 of Lactotransferrin
Cysteine 56 of Lactotransferrin
2pms B 116 B 199
A redox-regulated disulphide may form within Lactotransferrin between cysteines 135 and 218 (116 and 199 respectively in this structure).
Details
Redox score ?
79
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
135
Residue number B
218
Peptide name
Lactotransferrin
Ligandability
Cysteine 135 of Lactotransferrin
Cysteine 218 of Lactotransferrin
2pms A 174 A 182
A redox-regulated disulphide may form within Lactotransferrin between cysteines 193 and 201 (174 and 182 respectively in this structure).
Details
Redox score ?
74
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
193
Residue number B
201
Peptide name
Lactotransferrin
Ligandability
Cysteine 193 of Lactotransferrin
Cysteine 201 of Lactotransferrin
2pms B 171 B 174
A redox-regulated disulphide may form within Lactotransferrin between cysteines 190 and 193 (171 and 174 respectively in this structure).
Details
Redox score ?
66
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
87
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
190
Residue number B
193
Peptide name
Lactotransferrin
Ligandability
Cysteine 190 of Lactotransferrin
Cysteine 193 of Lactotransferrin
2pms B 158 B 182
A redox-regulated disulphide may form within Lactotransferrin between cysteines 177 and 201 (158 and 182 respectively in this structure).
Details
Redox score ?
61
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
5
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
177
Residue number B
201
Peptide name
Lactotransferrin
Ligandability
Cysteine 177 of Lactotransferrin
Cysteine 201 of Lactotransferrin
2pms B 158 B 199
A redox-regulated disulphide may form within Lactotransferrin between cysteines 177 and 218 (158 and 199 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
57
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
6
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
177
Residue number B
218
Peptide name
Lactotransferrin
Ligandability
Cysteine 177 of Lactotransferrin
Cysteine 218 of Lactotransferrin
2pms A 174 A 199
A redox-regulated disulphide may form within Lactotransferrin between cysteines 193 and 218 (174 and 199 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
193
Residue number B
218
Peptide name
Lactotransferrin
Ligandability
Cysteine 193 of Lactotransferrin
Cysteine 218 of Lactotransferrin
2pms B 158 B 171
A redox-regulated disulphide may form within Lactotransferrin between cysteines 177 and 190 (158 and 171 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
51
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
177
Residue number B
190
Peptide name
Lactotransferrin
Ligandability
Cysteine 177 of Lactotransferrin
Cysteine 190 of Lactotransferrin
2pms A 116 A 158
A redox-regulated disulphide may form within Lactotransferrin between cysteines 135 and 177 (116 and 158 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
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
7
Half-sphere exposure sum ?
105
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
135
Residue number B
177
Peptide name
Lactotransferrin
Ligandability
Cysteine 135 of Lactotransferrin
Cysteine 177 of Lactotransferrin
2pms B 116 B 174
A redox-regulated disulphide may form within Lactotransferrin between cysteines 135 and 193 (116 and 174 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
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
135
Residue number B
193
Peptide name
Lactotransferrin
Ligandability
Cysteine 135 of Lactotransferrin
Cysteine 193 of Lactotransferrin
2pms A 10 A 20
A redox-regulated disulphide may form within Lactotransferrin between cysteines 29 and 39 (10 and 20 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
29
Residue number B
39
Peptide name
Lactotransferrin
Ligandability
Cysteine 29 of Lactotransferrin
Cysteine 39 of Lactotransferrin
2pms A 20 A 46
A redox-regulated disulphide may form within Lactotransferrin between cysteines 39 and 65 (20 and 46 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
39
Residue number B
65
Peptide name
Lactotransferrin
Ligandability
Cysteine 39 of Lactotransferrin
Cysteine 65 of Lactotransferrin
2pms A 10 A 37
A redox-regulated disulphide may form within Lactotransferrin between cysteines 29 and 56 (10 and 37 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
2pms
Structure name
crystal structure of the complex of human lactoferrin n-lobe and lactoferrin-binding domain of pneumococcal surface protein a
Structure deposition date
2007-04-23
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q5EK51
Residue number A
29
Residue number B
56
Peptide name
Lactotransferrin
Ligandability
Cysteine 29 of Lactotransferrin
Cysteine 56 of Lactotransferrin
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