All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Intermolecular
Cysteine 101 and cysteine 287
Intramolecular
Cysteine 98 and cysteine 101
Cysteine 101 and cysteine 104
Cysteine 101 and cysteine 112
Cysteine 98 and cysteine 104
Cysteine 98 and cysteine 112
Cysteine 104 and cysteine 112
Cysteine 196 and cysteine 212
Cysteine 47 and cysteine 175
Cysteine 282 and cysteine 283
More...Cysteine 175 and cysteine 196
Cysteine 10 and cysteine 133
Cysteine 283 and cysteine 287
Cysteine 47 and cysteine 196
Cysteine 171 and cysteine 196
1hdz A 100 B 286
A redox-regulated disulphide may form between two units of All-trans-retinol dehydrogenase [NAD(+)] ADH1B at cysteines 101 and 287 (100 and 286 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
1hdz
Structure name
three-dimensional structures of three human alcohol dehydrogenase variants: correlations with their functional differences
Structure deposition date
1993-10-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
7
% buried
55
Peptide A name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Peptide B name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Peptide A accession
P00325
Peptide B accession
P00325
Peptide A residue number
101
Peptide B residue number
287
Ligandability
Cysteine 101 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 287 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1htb B 97 B 100
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 98 and 101 (97 and 100 respectively in this structure).
Details
Redox score ?
85
PDB code
1htb
Structure name
crystallization of human beta3 alcohol dehydrogenase (10 mg/ml) in 100 mm sodium phosphate (ph 7
Structure deposition date
1995-08-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
5
% buried
27
Peptide accession
P00325
Residue number A
98
Residue number B
101
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 98 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 101 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1htb B 100 B 103
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 101 and 104 (100 and 103 respectively in this structure).
Details
Redox score ?
84
PDB code
1htb
Structure name
crystallization of human beta3 alcohol dehydrogenase (10 mg/ml) in 100 mm sodium phosphate (ph 7
Structure deposition date
1995-08-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
34
Peptide accession
P00325
Residue number A
101
Residue number B
104
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 101 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 104 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1hdx A 100 A 111
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 101 and 112 (100 and 111 respectively in this structure).
Details
Redox score ?
83
PDB code
1hdx
Structure name
three-dimensional structures of three human alcohol dehydrogenase variants: correlations with their functional differences
Structure deposition date
1993-10-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
61
Minimum pKa ?
6
% buried
43
Peptide accession
P00325
Residue number A
101
Residue number B
112
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 101 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 112 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1deh A 97 A 103
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 98 and 104 (97 and 103 respectively in this structure).
Details
Redox score ?
82
PDB code
1deh
Structure name
crystallization of human beta1 alcohol dehydrogenase (15 mg/ml) in 50 mm sodium phosphate (ph 7
Structure deposition date
1995-10-14
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
5
% buried
30
Peptide accession
P00325
Residue number A
98
Residue number B
104
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 98 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 104 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1hdz B 97 B 111
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 98 and 112 (97 and 111 respectively in this structure).
Details
Redox score ?
78
PDB code
1hdz
Structure name
three-dimensional structures of three human alcohol dehydrogenase variants: correlations with their functional differences
Structure deposition date
1993-10-15
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
46
Peptide accession
P00325
Residue number A
98
Residue number B
112
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 98 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 112 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1htb A 103 A 111
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 104 and 112 (103 and 111 respectively in this structure).
Details
Redox score ?
75
PDB code
1htb
Structure name
crystallization of human beta3 alcohol dehydrogenase (10 mg/ml) in 100 mm sodium phosphate (ph 7
Structure deposition date
1995-08-10
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
10
% buried
50
Peptide accession
P00325
Residue number A
104
Residue number B
112
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 104 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 112 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1u3u A 195 A 211
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 196 and 212 (195 and 211 respectively in this structure).
Details
Redox score ?
68
PDB code
1u3u
Structure name
crystal structure of human alcohol dehydrogenase beta-1-beta-1 isoform complexed with n-benzylformamide determined to 1
Structure deposition date
2004-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
96
Minimum pKa ?
9
% buried
96
Peptide accession
P00325
Residue number A
196
Residue number B
212
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 196 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 212 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1hdy B 46 B 174
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 47 and 175 (46 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 ?
57
PDB code
1hdy
Structure name
three-dimensional structures of three human alcohol dehydrogenase variants: correlations with their functional differences
Structure deposition date
1993-10-15
Thiol separation (Å)
3
Half-sphere exposure sum ?
90
Minimum pKa ?
16
% buried
nan
Peptide accession
P00325
Residue number A
47
Residue number B
175
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 47 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 175 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1hdx B 281 B 282
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 282 and 283 (281 and 282 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
1hdx
Structure name
three-dimensional structures of three human alcohol dehydrogenase variants: correlations with their functional differences
Structure deposition date
1993-10-15
Thiol separation (Å)
6
Half-sphere exposure sum ?
88
Minimum pKa ?
11
% buried
100
Peptide accession
P00325
Residue number A
282
Residue number B
283
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 282 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 283 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1htb A 174 A 369
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 175 and 196 (174 and 369 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
1htb
Structure name
crystallization of human beta3 alcohol dehydrogenase (10 mg/ml) in 100 mm sodium phosphate (ph 7
Structure deposition date
1995-08-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
7
% buried
100
Peptide accession
P00325
Residue number A
175
Residue number B
196
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 175 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 196 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1deh B 9 B 132
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 10 and 133 (9 and 132 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
36
PDB code
1deh
Structure name
crystallization of human beta1 alcohol dehydrogenase (15 mg/ml) in 50 mm sodium phosphate (ph 7
Structure deposition date
1995-10-14
Thiol separation (Å)
10
Half-sphere exposure sum ?
55
Minimum pKa ?
11
% buried
53
Peptide accession
P00325
Residue number A
10
Residue number B
133
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 10 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 133 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1hdx A 282 A 286
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 283 and 287 (282 and 286 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
35
PDB code
1hdx
Structure name
three-dimensional structures of three human alcohol dehydrogenase variants: correlations with their functional differences
Structure deposition date
1993-10-15
Thiol separation (Å)
9
Half-sphere exposure sum ?
86
Minimum pKa ?
10
% buried
86
Peptide accession
P00325
Residue number A
283
Residue number B
287
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 283 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 287 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1htb A 46 A 369
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 47 and 196 (46 and 369 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
1htb
Structure name
crystallization of human beta3 alcohol dehydrogenase (10 mg/ml) in 100 mm sodium phosphate (ph 7
Structure deposition date
1995-08-10
Thiol separation (Å)
9
Half-sphere exposure sum ?
85
Minimum pKa ?
12
% buried
100
Peptide accession
P00325
Residue number A
47
Residue number B
196
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 47 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 196 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
1htb A 170 A 369
A redox-regulated disulphide may form within All-trans-retinol dehydrogenase [NAD(+)] ADH1B between cysteines 171 and 196 (170 and 369 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
33
PDB code
1htb
Structure name
crystallization of human beta3 alcohol dehydrogenase (10 mg/ml) in 100 mm sodium phosphate (ph 7
Structure deposition date
1995-08-10
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
13
% buried
100
Peptide accession
P00325
Residue number A
171
Residue number B
196
Peptide name
All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Ligandability
Cysteine 171 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
Cysteine 196 of All-trans-retinol dehydrogenase [NAD(+)] ADH1B
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