Interleukin-17F
Intermolecular
Cysteine 129 of Interleukin-17A and cysteine 47
Cysteine 47 and cysteine 137
Cysteine 154 and cysteine 154
Cysteine 146 of Interleukin-17A and cysteine 154
Cysteine 99 of Interleukin-17A and cysteine 154
Cysteine 107 and cysteine 154
Cysteine 146 of Interleukin-17A and cysteine 107
Intramolecular
Cysteine 102 and cysteine 152
Cysteine 102 and cysteine 107
Cysteine 107 and cysteine 152
More...Cysteine 102 and cysteine 154
Cysteine 152 and cysteine 154
5n92 A 129 F 47
A redox-regulated disulphide may form between cysteine 129 of Interleukin-17A and cysteine 47 of Interleukin-17F.
Details
Redox score ?
90
PDB code
5n92
Structure name
crystal structure of human il-17af
Structure deposition date
2017-02-24
Thiol separation (Å)
2
Half-sphere exposure sum ?
39
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17A
Peptide B name
Interleukin-17F
Peptide A accession
Q16552
Peptide B accession
Q96PD4
Peptide A residue number
129
Peptide B residue number
47
Ligandability
Cysteine 129 of Interleukin-17A
Cysteine 47 of Interleukin-17F
6hgo C 47 D 137
A redox-regulated disulphide may form between two units of Interleukin-17F at cysteines 47 and 137.
Details
Redox score ?
89
PDB code
6hgo
Structure name
crystal structure of human il-17f
Structure deposition date
2018-08-23
Thiol separation (Å)
2
Half-sphere exposure sum ?
35
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17F
Peptide B name
Interleukin-17F
Peptide A accession
Q96PD4
Peptide B accession
Q96PD4
Peptide A residue number
47
Peptide B residue number
137
Ligandability
Cysteine 47 of Interleukin-17F
Cysteine 137 of Interleukin-17F
3jvf A 124 B 124
A redox-regulated disulphide may form between two units of Interleukin-17F at cysteines 154 and 154 (124 and 124 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
3jvf
Structure name
crystal structure of an interleukin-17 receptor complex
Structure deposition date
2009-09-16
Thiol separation (Å)
7
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17F
Peptide B name
Interleukin-17F
Peptide A accession
Q96PD4
Peptide B accession
Q96PD4
Peptide A residue number
154
Peptide B residue number
154
Ligandability
5nan A 146 F 154
A redox-regulated disulphide may form between cysteine 146 of Interleukin-17A and cysteine 154 of Interleukin-17F. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
5nan
Structure name
crystal structure of human il-17af in complex with human il-17ra
Structure deposition date
2017-02-28
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17A
Peptide B name
Interleukin-17F
Peptide A accession
Q16552
Peptide B accession
Q96PD4
Peptide A residue number
146
Peptide B residue number
154
Ligandability
Cysteine 146 of Interleukin-17A
Cysteine 154 of Interleukin-17F
5n92 A 99 F 154
A redox-regulated disulphide may form between cysteine 99 of Interleukin-17A and cysteine 154 of Interleukin-17F. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
5n92
Structure name
crystal structure of human il-17af
Structure deposition date
2017-02-24
Thiol separation (Å)
9
Half-sphere exposure sum ?
84
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17A
Peptide B name
Interleukin-17F
Peptide A accession
Q16552
Peptide B accession
Q96PD4
Peptide A residue number
99
Peptide B residue number
154
Ligandability
Cysteine 99 of Interleukin-17A
Cysteine 154 of Interleukin-17F
6hgo A 107 B 154
A redox-regulated disulphide may form between two units of Interleukin-17F at cysteines 107 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
41
PDB code
6hgo
Structure name
crystal structure of human il-17f
Structure deposition date
2018-08-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17F
Peptide B name
Interleukin-17F
Peptide A accession
Q96PD4
Peptide B accession
Q96PD4
Peptide A residue number
107
Peptide B residue number
154
Ligandability
Cysteine 107 of Interleukin-17F
Cysteine 154 of Interleukin-17F
5nan A 146 F 107
A redox-regulated disulphide may form between cysteine 146 of Interleukin-17A and cysteine 107 of Interleukin-17F. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5nan
Structure name
crystal structure of human il-17af in complex with human il-17ra
Structure deposition date
2017-02-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17A
Peptide B name
Interleukin-17F
Peptide A accession
Q16552
Peptide B accession
Q96PD4
Peptide A residue number
146
Peptide B residue number
107
Ligandability
Cysteine 146 of Interleukin-17A
Cysteine 107 of Interleukin-17F
3jvf A 72 A 122
A redox-regulated disulphide may form within Interleukin-17F between cysteines 102 and 152 (72 and 122 respectively in this structure).
Details
Redox score ?
81
PDB code
3jvf
Structure name
crystal structure of an interleukin-17 receptor complex
Structure deposition date
2009-09-16
Thiol separation (Å)
2
Half-sphere exposure sum ?
79
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PD4
Residue number A
102
Residue number B
152
Peptide name
Interleukin-17F
Ligandability
Cysteine 102 of Interleukin-17F
Cysteine 152 of Interleukin-17F
6ppg F 72 F 77
A redox-regulated disulphide may form within Interleukin-17F between cysteines 102 and 107 (72 and 77 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
45
PDB code
6ppg
Structure name
crystal structure of il17ff bound to fab fragments of mcaf5352a
Structure deposition date
2019-07-06
Thiol separation (Å)
9
Half-sphere exposure sum ?
76
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PD4
Residue number A
102
Residue number B
107
Peptide name
Interleukin-17F
Ligandability
Cysteine 102 of Interleukin-17F
Cysteine 107 of Interleukin-17F
3jvf A 77 A 122
A redox-regulated disulphide may form within Interleukin-17F between cysteines 107 and 152 (77 and 122 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
3jvf
Structure name
crystal structure of an interleukin-17 receptor complex
Structure deposition date
2009-09-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PD4
Residue number A
107
Residue number B
152
Peptide name
Interleukin-17F
Ligandability
Cysteine 107 of Interleukin-17F
Cysteine 152 of Interleukin-17F
5nan E 102 E 154
A redox-regulated disulphide may form within Interleukin-17F between cysteines 102 and 154. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
5nan
Structure name
crystal structure of human il-17af in complex with human il-17ra
Structure deposition date
2017-02-28
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PD4
Residue number A
102
Residue number B
154
Peptide name
Interleukin-17F
Ligandability
Cysteine 102 of Interleukin-17F
Cysteine 154 of Interleukin-17F
3jvf A 122 A 124
A redox-regulated disulphide may form within Interleukin-17F between cysteines 152 and 154 (122 and 124 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3jvf
Structure name
crystal structure of an interleukin-17 receptor complex
Structure deposition date
2009-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
95
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q96PD4
Residue number A
152
Residue number B
154
Peptide name
Interleukin-17F
Ligandability
Cysteine 152 of Interleukin-17F
Cysteine 154 of Interleukin-17F
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