All-trans-retinol dehydrogenase [NAD(+)] ADH4
Intramolecular
Cysteine 102 and cysteine 105
Cysteine 99 and cysteine 102
Cysteine 102 and cysteine 113
Cysteine 99 and cysteine 105
Cysteine 99 and cysteine 113
Cysteine 105 and cysteine 113
Cysteine 201 and cysteine 217
Cysteine 47 and cysteine 180
Cysteine 45 and cysteine 175
Cysteine 23 and cysteine 138
More...Cysteine 287 and cysteine 295
Cysteine 10 and cysteine 137
Cysteine 47 and cysteine 207
Cysteine 179 and cysteine 207
Cysteine 217 and cysteine 274
Cysteine 200 and cysteine 286
Cysteine 175 and cysteine 207
Cysteine 45 and cysteine 70
Cysteine 273 and cysteine 294
Cysteine 207 and cysteine 273
Cysteine 45 and cysteine 179
3cos C 102 C 105
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 102 and 105.
Details
Redox score ?
88
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
48
Minimum pKa ?
5
% buried
32
Peptide accession
P08319
Residue number A
102
Residue number B
105
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 102 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 105 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos B 99 B 102
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 99 and 102.
Details
Redox score ?
85
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
45
Minimum pKa ?
5
% buried
18
Peptide accession
P08319
Residue number A
99
Residue number B
102
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 99 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 102 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos D 102 D 113
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 102 and 113.
Details
Redox score ?
82
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
57
Minimum pKa ?
5
% buried
36
Peptide accession
P08319
Residue number A
102
Residue number B
113
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 102 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 113 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos A 99 A 105
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 99 and 105.
Details
Redox score ?
79
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
56
Minimum pKa ?
7
% buried
24
Peptide accession
P08319
Residue number A
99
Residue number B
105
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 99 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 105 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos D 99 D 113
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 99 and 113.
Details
Redox score ?
77
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
65
Minimum pKa ?
7
% buried
32
Peptide accession
P08319
Residue number A
99
Residue number B
113
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 99 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 113 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos D 105 D 113
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 105 and 113.
Details
Redox score ?
75
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
68
Minimum pKa ?
10
% buried
44
Peptide accession
P08319
Residue number A
105
Residue number B
113
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 105 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 113 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos B 201 B 217
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 201 and 217.
Details
Redox score ?
70
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
96
Peptide accession
P08319
Residue number A
201
Residue number B
217
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 201 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 217 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos D 47 D 180
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 47 and 180.
Details
Redox score ?
65
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
4
Half-sphere exposure sum ?
90
Minimum pKa ?
8
% buried
100
Peptide accession
P08319
Residue number A
47
Residue number B
180
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 47 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 180 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3i A 44 A 174
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 45 and 175 (44 and 174 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
60
PDB code
1e3i
Structure name
mouse class ii alcohol dehydrogenase complex with nadh and inhibitor
Structure deposition date
2000-06-16
Thiol separation (Å)
4
Half-sphere exposure sum ?
106
Minimum pKa ?
9
% buried
100
Peptide accession
Q9QYY9
Residue number A
45
Residue number B
175
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 45 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 175 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos A 23 A 138
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 23 and 138. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
11
Peptide accession
P08319
Residue number A
23
Residue number B
138
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 23 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 138 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos C 287 C 295
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 287 and 295. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
39
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
7
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
P08319
Residue number A
287
Residue number B
295
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 287 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 295 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3l A 9 A 136
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 10 and 137 (9 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 ?
38
PDB code
1e3l
Structure name
p47h mutant of mouse class ii alcohol dehydrogenase complex with nadh
Structure deposition date
2000-06-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
56
Minimum pKa ?
10
% buried
54
Peptide accession
Q9QYY9
Residue number A
10
Residue number B
137
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 10 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 137 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3i A 46 A 206
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 47 and 207 (46 and 206 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
1e3i
Structure name
mouse class ii alcohol dehydrogenase complex with nadh and inhibitor
Structure deposition date
2000-06-16
Thiol separation (Å)
8
Half-sphere exposure sum ?
91
Minimum pKa ?
13
% buried
nan
Peptide accession
Q9QYY9
Residue number A
47
Residue number B
207
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 47 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 207 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3e A 178 A 206
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 179 and 207 (178 and 206 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
1e3e
Structure name
mouse class ii alcohol dehydrogenase complex with nadh
Structure deposition date
2000-06-14
Thiol separation (Å)
8
Half-sphere exposure sum ?
84
Minimum pKa ?
12
% buried
100
Peptide accession
Q9QYY9
Residue number A
179
Residue number B
207
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 179 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 207 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
3cos A 217 A 274
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 217 and 274. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
32
PDB code
3cos
Structure name
crystal structure of human class ii alcohol dehydrogenase (adh4) in complex with nad and zn
Structure deposition date
2008-03-29
Thiol separation (Å)
8
Half-sphere exposure sum ?
92
Minimum pKa ?
13
% buried
100
Peptide accession
P08319
Residue number A
217
Residue number B
274
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 217 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 274 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3l A 199 A 285
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 200 and 286 (199 and 285 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
1e3l
Structure name
p47h mutant of mouse class ii alcohol dehydrogenase complex with nadh
Structure deposition date
2000-06-19
Thiol separation (Å)
10
Half-sphere exposure sum ?
94
Minimum pKa ?
9
% buried
94
Peptide accession
Q9QYY9
Residue number A
200
Residue number B
286
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 200 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 286 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3i A 174 A 206
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 175 and 207 (174 and 206 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
1e3i
Structure name
mouse class ii alcohol dehydrogenase complex with nadh and inhibitor
Structure deposition date
2000-06-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
100
Peptide accession
Q9QYY9
Residue number A
175
Residue number B
207
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 175 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 207 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3i A 44 A 69
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 45 and 70 (44 and 69 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
24
PDB code
1e3i
Structure name
mouse class ii alcohol dehydrogenase complex with nadh and inhibitor
Structure deposition date
2000-06-16
Thiol separation (Å)
9
Half-sphere exposure sum ?
105
Minimum pKa ?
13
% buried
100
Peptide accession
Q9QYY9
Residue number A
45
Residue number B
70
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 45 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 70 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3i A 272 A 293
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 273 and 294 (272 and 293 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
22
PDB code
1e3i
Structure name
mouse class ii alcohol dehydrogenase complex with nadh and inhibitor
Structure deposition date
2000-06-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
97
Minimum pKa ?
12
% buried
100
Peptide accession
Q9QYY9
Residue number A
273
Residue number B
294
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 273 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 294 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3i A 206 A 272
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 207 and 273 (206 and 272 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
21
PDB code
1e3i
Structure name
mouse class ii alcohol dehydrogenase complex with nadh and inhibitor
Structure deposition date
2000-06-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
Q9QYY9
Residue number A
207
Residue number B
273
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 207 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 273 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
1e3i B 44 B 178
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH4 between cysteines 45 and 179 (44 and 178 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
13
PDB code
1e3i
Structure name
mouse class ii alcohol dehydrogenase complex with nadh and inhibitor
Structure deposition date
2000-06-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
103
Minimum pKa ?
16
% buried
100
Peptide accession
Q9QYY9
Residue number A
45
Residue number B
179
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH4
Ligandability
Cysteine 45 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
Cysteine 179 of All-trans-retinol dehydrogenase [NAD(+)] ADH4
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