Folate receptor alpha
Intramolecular
Cysteine 89 and cysteine 175
Cysteine 96 and cysteine 146
Cysteine 152 and cysteine 169
Cysteine 57 and cysteine 105
Cysteine 139 and cysteine 189
Cysteine 135 and cysteine 209
Cysteine 37 and cysteine 65
Cysteine 66 and cysteine 109
Cysteine 89 and cysteine 169
Cysteine 169 and cysteine 175
More...Cysteine 89 and cysteine 152
Cysteine 152 and cysteine 175
Cysteine 57 and cysteine 109
Cysteine 105 and cysteine 109
Cysteine 57 and cysteine 66
Cysteine 66 and cysteine 105
Cysteine 65 and cysteine 66
Cysteine 65 and cysteine 109
Cysteine 37 and cysteine 109
Cysteine 146 and cysteine 189
Cysteine 37 and cysteine 66
5izq B 67 B 153
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 89 and 175 (67 and 153 respectively in this structure).
Details
Redox score ?
86
PDB code
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
49
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
89
Residue number B
175
Peptide name
Folate receptor alpha
Ligandability
Cysteine 89 of Folate receptor alpha
Cysteine 175 of Folate receptor alpha
4lrh E 74 E 124
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 96 and 146 (74 and 124 respectively in this structure).
Details
Redox score ?
84
PDB code
4lrh
Structure name
crystal structure of human folate receptor alpha in complex with folic acid
Structure deposition date
2013-07-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
60
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
96
Residue number B
146
Peptide name
Folate receptor alpha
Ligandability
Cysteine 96 of Folate receptor alpha
Cysteine 146 of Folate receptor alpha
5izq D 130 D 147
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 152 and 169 (130 and 147 respectively in this structure).
Details
Redox score ?
82
PDB code
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
152
Residue number B
169
Peptide name
Folate receptor alpha
Ligandability
Cysteine 152 of Folate receptor alpha
Cysteine 169 of Folate receptor alpha
5izq F 35 F 83
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 57 and 105 (35 and 83 respectively in this structure).
Details
Redox score ?
82
PDB code
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
57
Residue number B
105
Peptide name
Folate receptor alpha
Ligandability
Cysteine 57 of Folate receptor alpha
Cysteine 105 of Folate receptor alpha
5izq E 117 E 167
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 139 and 189 (117 and 167 respectively in this structure).
Details
Redox score ?
81
PDB code
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
82
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
139
Residue number B
189
Peptide name
Folate receptor alpha
Ligandability
Cysteine 139 of Folate receptor alpha
Cysteine 189 of Folate receptor alpha
5izq A 113 A 187
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 135 and 209 (113 and 187 respectively in this structure).
Details
Redox score ?
81
PDB code
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
2
Half-sphere exposure sum ?
71
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
135
Residue number B
209
Peptide name
Folate receptor alpha
Ligandability
Cysteine 135 of Folate receptor alpha
Cysteine 209 of Folate receptor alpha
4lrh F 15 F 43
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 37 and 65 (15 and 43 respectively in this structure).
Details
Redox score ?
79
PDB code
4lrh
Structure name
crystal structure of human folate receptor alpha in complex with folic acid
Structure deposition date
2013-07-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
37
Residue number B
65
Peptide name
Folate receptor alpha
Ligandability
Cysteine 37 of Folate receptor alpha
Cysteine 65 of Folate receptor alpha
4lrh B 44 B 87
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 66 and 109 (44 and 87 respectively in this structure).
Details
Redox score ?
79
PDB code
4lrh
Structure name
crystal structure of human folate receptor alpha in complex with folic acid
Structure deposition date
2013-07-19
Thiol separation (Å)
2
Half-sphere exposure sum ?
91
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
66
Residue number B
109
Peptide name
Folate receptor alpha
Ligandability
Cysteine 66 of Folate receptor alpha
Cysteine 109 of Folate receptor alpha
4lrh D 67 D 147
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 89 and 169 (67 and 147 respectively in this structure).
Details
Redox score ?
77
PDB code
4lrh
Structure name
crystal structure of human folate receptor alpha in complex with folic acid
Structure deposition date
2013-07-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
89
Residue number B
169
Peptide name
Folate receptor alpha
Ligandability
Cysteine 89 of Folate receptor alpha
Cysteine 169 of Folate receptor alpha
4lrh F 147 F 153
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 169 and 175 (147 and 153 respectively in this structure).
Details
Redox score ?
72
PDB code
4lrh
Structure name
crystal structure of human folate receptor alpha in complex with folic acid
Structure deposition date
2013-07-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
54
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
169
Residue number B
175
Peptide name
Folate receptor alpha
Ligandability
Cysteine 169 of Folate receptor alpha
Cysteine 175 of Folate receptor alpha
4lrh C 67 C 130
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 89 and 152 (67 and 130 respectively in this structure).
Details
Redox score ?
70
PDB code
4lrh
Structure name
crystal structure of human folate receptor alpha in complex with folic acid
Structure deposition date
2013-07-19
Thiol separation (Å)
4
Half-sphere exposure sum ?
63
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
89
Residue number B
152
Peptide name
Folate receptor alpha
Ligandability
Cysteine 89 of Folate receptor alpha
Cysteine 152 of Folate receptor alpha
5izq H 130 H 153
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 152 and 175 (130 and 153 respectively in this structure).
Details
Redox score ?
68
PDB code
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
55
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
152
Residue number B
175
Peptide name
Folate receptor alpha
Ligandability
Cysteine 152 of Folate receptor alpha
Cysteine 175 of Folate receptor alpha
5izq B 35 B 87
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 57 and 109 (35 and 87 respectively in this structure).
Details
Redox score ?
67
PDB code
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
4
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
57
Residue number B
109
Peptide name
Folate receptor alpha
Ligandability
Cysteine 57 of Folate receptor alpha
Cysteine 109 of Folate receptor alpha
5izq H 83 H 87
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 105 and 109 (83 and 87 respectively in this structure).
Details
Redox score ?
64
PDB code
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
5
Half-sphere exposure sum ?
88
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
105
Residue number B
109
Peptide name
Folate receptor alpha
Ligandability
Cysteine 105 of Folate receptor alpha
Cysteine 109 of Folate receptor alpha
4kmx A 57 A 66
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 57 and 66.
Details
Redox score ?
63
PDB code
4kmx
Structure name
human folate receptor alpha (folr1) at acidic ph, hexagonal form
Structure deposition date
2013-05-08
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
57
Residue number B
66
Peptide name
Folate receptor alpha
Ligandability
Cysteine 57 of Folate receptor alpha
Cysteine 66 of Folate receptor alpha
4kmx A 66 A 105
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 66 and 105. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
52
PDB code
4kmx
Structure name
human folate receptor alpha (folr1) at acidic ph, hexagonal form
Structure deposition date
2013-05-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
66
Residue number B
105
Peptide name
Folate receptor alpha
Ligandability
Cysteine 66 of Folate receptor alpha
Cysteine 105 of Folate receptor alpha
4km7 B 65 B 66
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 65 and 66. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
4km7
Structure name
human folate receptor alpha (folr1) at acidic ph, triclinic form
Structure deposition date
2013-05-08
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
65
Residue number B
66
Peptide name
Folate receptor alpha
Ligandability
Cysteine 65 of Folate receptor alpha
Cysteine 66 of Folate receptor alpha
4km7 B 65 B 109
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 65 and 109. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
4km7
Structure name
human folate receptor alpha (folr1) at acidic ph, triclinic form
Structure deposition date
2013-05-08
Thiol separation (Å)
8
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
65
Residue number B
109
Peptide name
Folate receptor alpha
Ligandability
Cysteine 65 of Folate receptor alpha
Cysteine 109 of Folate receptor alpha
5izq E 15 E 87
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 37 and 109 (15 and 87 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
5izq
Structure name
crystal structure of human folate receptor alpha in complex with novel antifolate agf183
Structure deposition date
2016-03-25
Thiol separation (Å)
9
Half-sphere exposure sum ?
83
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
37
Residue number B
109
Peptide name
Folate receptor alpha
Ligandability
Cysteine 37 of Folate receptor alpha
Cysteine 109 of Folate receptor alpha
4lrh D 124 D 167
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 146 and 189 (124 and 167 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4lrh
Structure name
crystal structure of human folate receptor alpha in complex with folic acid
Structure deposition date
2013-07-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
146
Residue number B
189
Peptide name
Folate receptor alpha
Ligandability
Cysteine 146 of Folate receptor alpha
Cysteine 189 of Folate receptor alpha
4lrh E 15 E 44
A redox-regulated disulphide may form within Folate receptor alpha between cysteines 37 and 66 (15 and 44 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
4lrh
Structure name
crystal structure of human folate receptor alpha in complex with folic acid
Structure deposition date
2013-07-19
Thiol separation (Å)
9
Half-sphere exposure sum ?
81
Minimum pKa ?
nan
% buried
nan
Peptide accession
P15328
Residue number A
37
Residue number B
66
Peptide name
Folate receptor alpha
Ligandability
Cysteine 37 of Folate receptor alpha
Cysteine 66 of Folate receptor alpha
If this tool was useful for finding a disulphide, please cite: