Interleukin-17A
Intermolecular
Cysteine 129 and cysteine 47 of Interleukin-17F
Cysteine 146 and cysteine 146
Cysteine 146 and cysteine 154 of Interleukin-17F
Cysteine 99 and cysteine 154 of Interleukin-17F
Cysteine 99 and cysteine 146
Cysteine 99 and cysteine 99
Cysteine 146 and cysteine 107 of Interleukin-17F
Intramolecular
Cysteine 33 and cysteine 129
Cysteine 94 and cysteine 144
Cysteine 94 and cysteine 99
More...Cysteine 99 and cysteine 144
Cysteine 94 and cysteine 146
Cysteine 144 and cysteine 146
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
5n7w X 123 Y 123
A redox-regulated disulphide may form between two units of Interleukin-17A at cysteines 146 and 146 (123 and 123 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
5n7w
Structure name
computationally designed functional antibody
Structure deposition date
2017-02-21
Thiol separation (Å)
7
Half-sphere exposure sum ?
96
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17A
Peptide B name
Interleukin-17A
Peptide A accession
Q16552
Peptide B accession
Q16552
Peptide A residue number
146
Peptide B residue number
146
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
5hi5 A 76 B 123
A redox-regulated disulphide may form between two units of Interleukin-17A at cysteines 99 and 146 (76 and 123 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
5hi5
Structure name
binding site elucidation and structure guided design of macrocyclic il-17a antagonists
Structure deposition date
2016-01-11
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17A
Peptide B name
Interleukin-17A
Peptide A accession
Q16552
Peptide B accession
Q16552
Peptide A residue number
99
Peptide B residue number
146
Ligandability
Cysteine 99 of Interleukin-17A
Cysteine 146 of Interleukin-17A
7uwn A 99 B 99
A redox-regulated disulphide may form between two units of Interleukin-17A at cysteines 99 and 99. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
7uwn
Structure name
structure of the il-17a-il-17ra-il-17rc ternary complex
Structure deposition date
2022-05-03
Thiol separation (Å)
10
Half-sphere exposure sum ?
78
Minimum pKa ?
nan
% buried
nan
Peptide A name
Interleukin-17A
Peptide B name
Interleukin-17A
Peptide A accession
Q16552
Peptide B accession
Q16552
Peptide A residue number
99
Peptide B residue number
99
Ligandability
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
5n7w X 10 X 106
A redox-regulated disulphide may form within Interleukin-17A between cysteines 33 and 129 (10 and 106 respectively in this structure).
Details
Redox score ?
85
PDB code
5n7w
Structure name
computationally designed functional antibody
Structure deposition date
2017-02-21
Thiol separation (Å)
2
Half-sphere exposure sum ?
52
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16552
Residue number A
33
Residue number B
129
Peptide name
Interleukin-17A
Ligandability
Cysteine 33 of Interleukin-17A
Cysteine 129 of Interleukin-17A
8dyi B 94 B 144
A redox-regulated disulphide may form within Interleukin-17A between cysteines 94 and 144.
Details
Redox score ?
81
PDB code
8dyi
Structure name
il17a homodimer bound to compound 5
Structure deposition date
2022-08-04
Thiol separation (Å)
2
Half-sphere exposure sum ?
80
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16552
Residue number A
94
Residue number B
144
Peptide name
Interleukin-17A
Ligandability
Cysteine 94 of Interleukin-17A
Cysteine 144 of Interleukin-17A
5vb9 A 71 A 76
A redox-regulated disulphide may form within Interleukin-17A between cysteines 94 and 99 (71 and 76 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
5vb9
Structure name
il-17a in complex with peptide
Structure deposition date
2017-03-28
Thiol separation (Å)
9
Half-sphere exposure sum ?
62
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16552
Residue number A
94
Residue number B
99
Peptide name
Interleukin-17A
Ligandability
Cysteine 94 of Interleukin-17A
Cysteine 99 of Interleukin-17A
5nan D 99 D 144
A redox-regulated disulphide may form within Interleukin-17A between cysteines 99 and 144. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
40
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 accession
Q16552
Residue number A
99
Residue number B
144
Peptide name
Interleukin-17A
Ligandability
Cysteine 99 of Interleukin-17A
Cysteine 144 of Interleukin-17A
8dyf A 94 A 146
A redox-regulated disulphide may form within Interleukin-17A between cysteines 94 and 146. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
8dyf
Structure name
il17a homodimer bound to compound 10
Structure deposition date
2022-08-04
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16552
Residue number A
94
Residue number B
146
Peptide name
Interleukin-17A
Ligandability
Cysteine 94 of Interleukin-17A
Cysteine 146 of Interleukin-17A
5nan D 144 D 146
A redox-regulated disulphide may form within Interleukin-17A between cysteines 144 and 146. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
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 ?
97
Minimum pKa ?
nan
% buried
nan
Peptide accession
Q16552
Residue number A
144
Residue number B
146
Peptide name
Interleukin-17A
Ligandability
Cysteine 144 of Interleukin-17A
Cysteine 146 of Interleukin-17A
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