Myeloid differentiation primary response protein MyD88
Intramolecular
Cysteine 166 and cysteine 233
Cysteine 192 and cysteine 216
Cysteine 168 and cysteine 233
Cysteine 274 and cysteine 280 L
Cysteine 192 and cysteine 203
Cysteine 166 and cysteine 216
Cysteine 166 and cysteine 168
Cysteine 166 and cysteine 192
7l6w A 166 A 233
A redox-regulated disulphide may form within Myeloid differentiation primary response protein MyD88 between cysteines 166 and 233.
Details
Redox score ?
74
PDB code
7l6w
Structure name
sfx structure of the myd88 tir domain higher-order assembly
Structure deposition date
2020-12-24
Thiol separation (Å)
4
Half-sphere exposure sum ?
75
Minimum pKa ?
7
% buried
84
Peptide accession
Q99836
Residue number A
166
Residue number B
233
Peptide name
Myeloid differentiation primary response protein MyD88
Ligandability
Cysteine 166 of Myeloid differentiation primary response protein MyD88
Cysteine 233 of Myeloid differentiation primary response protein MyD88
2js7 A 48 A 72
A redox-regulated disulphide may form within Myeloid differentiation primary response protein MyD88 between cysteines 192 and 216 (48 and 72 respectively in this structure).
Details
Redox score ?
73
PDB code
2js7
Structure name
solution nmr structure of human myeloid differentiation primary response (myd88)
Structure deposition date
2007-06-29
Thiol separation (Å)
3
Half-sphere exposure sum ?
71
Minimum pKa ?
11
% buried
78
Peptide accession
Q99836
Residue number A
192
Residue number B
216
Peptide name
Myeloid differentiation primary response protein MyD88
Ligandability
Cysteine 192 of Myeloid differentiation primary response protein MyD88
Cysteine 216 of Myeloid differentiation primary response protein MyD88
4eo7 A 168 A 233
A redox-regulated disulphide may form within Myeloid differentiation primary response protein MyD88 between cysteines 168 and 233. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
46
PDB code
4eo7
Structure name
crystal structure of the tir domain of human myeloid differentiation primary response protein 88
Structure deposition date
2012-04-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
63
Minimum pKa ?
10
% buried
40
Peptide accession
Q99836
Residue number A
168
Residue number B
233
Peptide name
Myeloid differentiation primary response protein MyD88
Ligandability
Cysteine 168 of Myeloid differentiation primary response protein MyD88
Cysteine 233 of Myeloid differentiation primary response protein MyD88
2js7 A 130 A 136
A redox-regulated disulphide may form within Myeloid differentiation primary response protein MyD88 between cysteines 274 and 280 (130 and 136 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
2js7
Structure name
solution nmr structure of human myeloid differentiation primary response (myd88)
Structure deposition date
2007-06-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
44
Minimum pKa ?
9
% buried
30
Peptide accession
Q99836
Residue number A
274
Residue number B
280
Peptide name
Myeloid differentiation primary response protein MyD88
Ligandability
Cysteine 274 of Myeloid differentiation primary response protein MyD88
Cysteine 280 of Myeloid differentiation primary response protein MyD88
2js7 A 48 A 59
A redox-regulated disulphide may form within Myeloid differentiation primary response protein MyD88 between cysteines 192 and 203 (48 and 59 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
2js7
Structure name
solution nmr structure of human myeloid differentiation primary response (myd88)
Structure deposition date
2007-06-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
59
Minimum pKa ?
10
% buried
48
Peptide accession
Q99836
Residue number A
192
Residue number B
203
Peptide name
Myeloid differentiation primary response protein MyD88
Ligandability
Cysteine 192 of Myeloid differentiation primary response protein MyD88
Cysteine 203 of Myeloid differentiation primary response protein MyD88
2js7 A 22 A 72
A redox-regulated disulphide may form within Myeloid differentiation primary response protein MyD88 between cysteines 166 and 216 (22 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
2js7
Structure name
solution nmr structure of human myeloid differentiation primary response (myd88)
Structure deposition date
2007-06-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
88
Peptide accession
Q99836
Residue number A
166
Residue number B
216
Peptide name
Myeloid differentiation primary response protein MyD88
Ligandability
Cysteine 166 of Myeloid differentiation primary response protein MyD88
Cysteine 216 of Myeloid differentiation primary response protein MyD88
4eo7 A 166 A 168
A redox-regulated disulphide may form within Myeloid differentiation primary response protein MyD88 between cysteines 166 and 168. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
38
PDB code
4eo7
Structure name
crystal structure of the tir domain of human myeloid differentiation primary response protein 88
Structure deposition date
2012-04-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
73
Minimum pKa ?
11
% buried
66
Peptide accession
Q99836
Residue number A
166
Residue number B
168
Peptide name
Myeloid differentiation primary response protein MyD88
Ligandability
Cysteine 166 of Myeloid differentiation primary response protein MyD88
Cysteine 168 of Myeloid differentiation primary response protein MyD88
2js7 A 22 A 48
A redox-regulated disulphide may form within Myeloid differentiation primary response protein MyD88 between cysteines 166 and 192 (22 and 48 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
31
PDB code
2js7
Structure name
solution nmr structure of human myeloid differentiation primary response (myd88)
Structure deposition date
2007-06-29
Thiol separation (Å)
9
Half-sphere exposure sum ?
77
Minimum pKa ?
13
% buried
86
Peptide accession
Q99836
Residue number A
166
Residue number B
192
Peptide name
Myeloid differentiation primary response protein MyD88
Ligandability
Cysteine 166 of Myeloid differentiation primary response protein MyD88
Cysteine 192 of Myeloid differentiation primary response protein MyD88
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