ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

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Alcohol dehydrogenase 1C

Intermolecular
Cysteine 101 and cysteine 287
Intramolecular
Cysteine 104 and cysteine 112
Cysteine 101 and cysteine 112
Cysteine 101 and cysteine 104
Cysteine 98 and cysteine 101
Cysteine 98 and cysteine 112
Cysteine 98 and cysteine 104
Cysteine 196 and cysteine 212
Cysteine 47 and cysteine 175
Cysteine 282 and cysteine 283
Cysteine 283 and cysteine 287
A redox-regulated disulphide may form between two units of Alcohol dehydrogenase 1C 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 ?
39
PDB code
1u3w
Structure name
crystal structure of human alcohol dehydrogenase gamma-2-gamma-2 isoform complexed with n-1-methylheptylformamide determined to 1
Structure deposition date
2004-07-23
Thiol separation (Å)
9
Half-sphere exposure sum ?
68
Minimum pKa ?
9
% buried
57
Peptide A name
Alcohol dehydrogenase 1C
Peptide B name
Alcohol dehydrogenase 1C
Peptide A accession
P00326
Peptide B accession
P00326
Peptide A residue number
101
Peptide B residue number
287

Ligandability

Cysteine 101 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 287 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C between cysteines 104 and 112 (103 and 111 respectively in this structure).

Details

Redox score ?
87
PDB code
1ht0
Structure name
human gamma-2 alcohol dehydrogense
Structure deposition date
2000-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
69
Minimum pKa ?
4
% buried
52
Peptide accession
P00326
Residue number A
104
Residue number B
112
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 104 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 112 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C between cysteines 101 and 112 (100 and 111 respectively in this structure).

Details

Redox score ?
85
PDB code
1ht0
Structure name
human gamma-2 alcohol dehydrogense
Structure deposition date
2000-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
62
Minimum pKa ?
4
% buried
46
Peptide accession
P00326
Residue number A
101
Residue number B
112
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 101 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 112 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C between cysteines 101 and 104 (100 and 103 respectively in this structure).

Details

Redox score ?
84
PDB code
1ht0
Structure name
human gamma-2 alcohol dehydrogense
Structure deposition date
2000-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
36
Peptide accession
P00326
Residue number A
101
Residue number B
104
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 101 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 104 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C between cysteines 98 and 101 (97 and 100 respectively in this structure).

Details

Redox score ?
79
PDB code
1u3w
Structure name
crystal structure of human alcohol dehydrogenase gamma-2-gamma-2 isoform complexed with n-1-methylheptylformamide determined to 1
Structure deposition date
2004-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
51
Minimum pKa ?
7
% buried
28
Peptide accession
P00326
Residue number A
98
Residue number B
101
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 98 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 101 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C between cysteines 98 and 112 (97 and 111 respectively in this structure).

Details

Redox score ?
76
PDB code
1u3w
Structure name
crystal structure of human alcohol dehydrogenase gamma-2-gamma-2 isoform complexed with n-1-methylheptylformamide determined to 1
Structure deposition date
2004-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
70
Minimum pKa ?
7
% buried
47
Peptide accession
P00326
Residue number A
98
Residue number B
112
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 98 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 112 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C between cysteines 98 and 104 (97 and 103 respectively in this structure).

Details

Redox score ?
76
PDB code
1ht0
Structure name
human gamma-2 alcohol dehydrogense
Structure deposition date
2000-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
58
Minimum pKa ?
9
% buried
34
Peptide accession
P00326
Residue number A
98
Residue number B
104
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 98 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 104 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C between cysteines 196 and 212 (195 and 211 respectively in this structure).

Details

Redox score ?
68
PDB code
1ht0
Structure name
human gamma-2 alcohol dehydrogense
Structure deposition date
2000-12-27
Thiol separation (Å)
4
Half-sphere exposure sum ?
97
Minimum pKa ?
9
% buried
94
Peptide accession
P00326
Residue number A
196
Residue number B
212
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 196 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 212 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C 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 ?
53
PDB code
1u3w
Structure name
crystal structure of human alcohol dehydrogenase gamma-2-gamma-2 isoform complexed with n-1-methylheptylformamide determined to 1
Structure deposition date
2004-07-23
Thiol separation (Å)
4
Half-sphere exposure sum ?
94
Minimum pKa ?
16
% buried
nan
Peptide accession
P00326
Residue number A
47
Residue number B
175
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 47 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 175 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C 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 ?
49
PDB code
1ht0
Structure name
human gamma-2 alcohol dehydrogense
Structure deposition date
2000-12-27
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
11
% buried
100
Peptide accession
P00326
Residue number A
282
Residue number B
283
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 282 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 283 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

A redox-regulated disulphide may form within Alcohol dehydrogenase 1C 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 ?
36
PDB code
1ht0
Structure name
human gamma-2 alcohol dehydrogense
Structure deposition date
2000-12-27
Thiol separation (Å)
8
Half-sphere exposure sum ?
90
Minimum pKa ?
11
% buried
90
Peptide accession
P00326
Residue number A
283
Residue number B
287
Peptide name
Alcohol dehydrogenase 1C

Ligandability

Cysteine 283 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

Cysteine 287 of Alcohol dehydrogenase 1C

Not ligandable in the dataset of Yang et al.

Not ligandable in the dataset of Yan et al.

Not ligandable in the dataset of Backus et al.

Not ligandable in the dataset of Vinogradova et al.

Not ligandable in the dataset of Cao et al.

Not ligandable in the dataset of Kuljanin et al.

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