NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Intermolecular
Cysteine 179 and cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Cysteine 182 and cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Intramolecular
Cysteine 143 and cysteine 189
Cysteine 150 and cysteine 179
Cysteine 146 and cysteine 189
Cysteine 150 and cysteine 182
Cysteine 150 and cysteine 185
Cysteine 140 and cysteine 189
Cysteine 140 and cysteine 146
Cysteine 143 and cysteine 146
More...Cysteine 182 and cysteine 185
Cysteine 179 and cysteine 182
Cysteine 140 and cysteine 143
Cysteine 146 and cysteine 150
Cysteine 146 and cysteine 185
Cysteine 179 and cysteine 185
Cysteine 185 and cysteine 189
7vxu B 152 C 166
A redox-regulated disulphide may form between cysteine 179 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial and cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (152 and 166 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
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
100
Peptide A name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Peptide B name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Peptide A accession
A0A4X1SVK9
Peptide B accession
A0A4X1VTL7
Peptide A residue number
179
Peptide B residue number
233
Ligandability
Cysteine 179 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu B 155 C 166
A redox-regulated disulphide may form between cysteine 182 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial and cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (155 and 166 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
10
% buried
100
Peptide A name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Peptide B name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Peptide A accession
A0A4X1SVK9
Peptide B accession
A0A4X1VTL7
Peptide A residue number
182
Peptide B residue number
233
Ligandability
Cysteine 182 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu B 116 B 162
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 143 and 189 (116 and 162 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
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
10
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
143
Residue number B
189
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 143 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 189 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 123 B 152
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 150 and 179 (123 and 152 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
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
150
Residue number B
179
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 150 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 179 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 119 B 162
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 146 and 189 (119 and 162 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
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
81
Minimum pKa ?
10
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
146
Residue number B
189
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 146 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 189 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 123 B 155
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 150 and 182 (123 and 155 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
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
11
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
150
Residue number B
182
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 150 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 182 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 123 B 158
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 150 and 185 (123 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 ?
49
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
78
Minimum pKa ?
11
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
150
Residue number B
185
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 150 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 185 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 113 B 162
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 140 and 189 (113 and 162 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
82
Minimum pKa ?
10
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
140
Residue number B
189
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 140 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 189 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 113 B 119
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 140 and 146 (113 and 119 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
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
140
Residue number B
146
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 140 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 146 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 116 B 119
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 143 and 146 (116 and 119 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
44
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
88
Minimum pKa ?
12
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
143
Residue number B
146
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 143 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 146 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 155 B 158
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 182 and 185 (155 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 ?
43
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
86
Minimum pKa ?
13
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
182
Residue number B
185
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 182 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 185 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 152 B 155
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 179 and 182 (152 and 155 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
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
179
Residue number B
182
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 179 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 182 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 113 B 116
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 140 and 143 (113 and 116 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
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
12
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
140
Residue number B
143
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 140 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 143 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 119 B 123
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 146 and 150 (119 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 ?
40
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
81
Minimum pKa ?
11
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
146
Residue number B
150
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 146 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 150 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 119 B 158
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 146 and 185 (119 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 ?
39
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
81
Minimum pKa ?
15
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
146
Residue number B
185
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 146 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 185 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 152 B 158
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 179 and 185 (152 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 ?
39
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
82
Minimum pKa ?
16
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
179
Residue number B
185
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 179 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 185 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
7vxu B 158 B 162
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial between cysteines 185 and 189 (158 and 162 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
9
Half-sphere exposure sum ?
78
Minimum pKa ?
10
% buried
100
Peptide accession
A0A4X1SVK9
Residue number A
185
Residue number B
189
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Ligandability
Cysteine 185 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 189 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
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